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Entry version 78 (29 Sep 2021)
Sequence version 1 (05 Apr 2011)
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Protein

2'-5'-oligoadenylate synthase 2

Gene

Oas2

Organism
Mus musculus (Mouse)
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

Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:12396720, PubMed:29117179).

Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation (PubMed:29117179).

Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:21142819).

Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL (PubMed:21142819).

In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (PubMed:21142819).

May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (PubMed:29117179).

Non-infected lobules would not be affected, allowing efficient pup feeding during infection (PubMed:29117179).

1 Publication3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Produced as a latent enzyme which is activated by double stranded RNA (dsRNA) generated during the course of viral infection (PubMed:29117179). The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated (By similarity). ssRNA or dsDNA do not act as activators (By similarity). Strongly inhibited by copper, iron and zinc ions (By similarity). Partially inhibited by cobalt and nickel ions (By similarity).By similarity1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 6.4 sec(-1) for ATP.1 Publication
  1. KM=1.9 mM for ATP1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei436ATPBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi448Magnesium; catalyticSequence analysis1
Metal bindingi450Magnesium; catalyticSequence analysis1
Metal bindingi519Magnesium; catalyticSequence analysis1
Binding sitei582ATPBy similarity1
Binding sitei585ATPBy 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 functionNucleotidyltransferase, RNA-binding, Transferase
Biological processAntiviral defense, Immunity, Innate immunity
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-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:
2'-5'-oligoadenylate synthase 2 (EC:2.7.7.842 Publications)
Short name:
(2-5')oligo(A) synthase 2
Short name:
2-5A synthase 2
Alternative name(s):
2',5'-oligoadenylate synthetase-like 111 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Oas2Imported
Synonyms:oasl111 Publication
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Chromosome 5

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:2180852, Oas2

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSMUSG00000032690

<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

Cytoplasm

<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_and_biotech_section">'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>Mutagenesisi405I → N: Mice display postpartum failure of lactation and strongly reduced milk protein synthesis. Otherwise, mice develop normally and mammary glands are normal. The mutation causes an activation of the OAS2 pathway, characterized by a strong increase of Ribonuclease L (RNASEL) activity. 1 Publication1
Mutagenesisi444K → A or G: Strongly reduced 2'-5'-oligoadenylate synthase activity. 1 Publication1
Mutagenesisi509S → L: Abolished 2'-5'-oligoadenylate synthase activity. 1 Publication1
Mutagenesisi538P → L: Strongly reduced 2'-5'-oligoadenylate synthase activity. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00004186282 – 7422'-5'-oligoadenylate synthase 2Add BLAST741

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycineBy similarity1
<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 residuei417N6-acetyllysineBy 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

Myristoylation is not essential for its activity.By similarity
Glycosylated. Glycosylation is essential for its activity.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Lipoprotein, Myristate

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
E9Q9A9

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
E9Q9A9

MaxQB - The MaxQuant DataBase

More...
MaxQBi
E9Q9A9

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
E9Q9A9

PeptideAtlas

More...
PeptideAtlasi
E9Q9A9

PRoteomics IDEntifications database

More...
PRIDEi
E9Q9A9

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
289956 [E9Q9A9-1]
289957 [E9Q9A9-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
E9Q9A9

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
E9Q9A9

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
E9Q9A9

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the uterus (PubMed:12396720). Expressed in mammary glands: expressed at low level before the establishment of lactation, then expression strongly increases, and subsequently decreases during early involution (PubMed:29117179).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000032690, Expressed in bone marrow macrophage and 148 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
E9Q9A9, MM

<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

Homodimer.

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
232936, 10 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000060082

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
E9Q9A9, protein

<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
E9Q9A9

Database of comparative protein structure models

More...
ModBasei
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>Regioni1 – 35DisorderedSequence analysisAdd BLAST35
Regioni60 – 374OAS domain 1Add BLAST315
Regioni382 – 721OAS domain 2Add BLAST340

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 – 26Polar residuesSequence analysisAdd BLAST26

<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 2-5A synthase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502S649, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00510000046406

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_026275_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
E9Q9A9

Identification of Orthologs from Complete Genome Data

More...
OMAi
WMKDSFE

Database of Orthologous Groups

More...
OrthoDBi
611234at2759

TreeFam database of animal gene trees

More...
TreeFami
TF329749

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05400, NT_2-5OAS_ClassI-CCAase, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.460.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018952, 2-5-oligoAdlate_synth_1_dom2/C
IPR026774, 2-5A_synthase
IPR006117, 2-5OAS_C_CS
IPR043518, 2-5OAS_N_CS
IPR006116, NT_2-5OAS_ClassI-CCAase
IPR043519, NT_sf
IPR002934, Polymerase_NTP_transf_dom

The PANTHER Classification System

More...
PANTHERi
PTHR11258, PTHR11258, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01909, NTP_transf_2, 1 hit
PF10421, OAS1_C, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81301, SSF81301, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00832, 25A_SYNTH_1, 1 hit
PS00833, 25A_SYNTH_2, 2 hits
PS50152, 25A_SYNTH_3, 2 hits

<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>. 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>Sequences (2+)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: E9Q9A9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGNWLTGNWS SDRSSGYSSG WSPGGSSGVP SGPVHKLEKS IQANLTPNEN
60 70 80 90 100
CLKQIAVSSV PSQKLEGYIQ ENLKPNRESL KQIDQAVDAI WDLLRSQIPV
110 120 130 140 150
KEVAKGGSYG RETALRGCSD GTLVLFMDCF QQFQDQIKYQ DAYLDVIELW
160 170 180 190 200
LKIHEKKSVK HEHALVVQVS VPGQRILLQL LPVFNPLRSN ENPSSCVYVD
210 220 230 240 250
LKKSMDQVRA SPGEFSDCFT TLQQRFFKKY PQRLKDLILL VKHWYEQCQE
260 270 280 290 300
KWKTPPPQPL LYALELLTVY AWEQGCQAED FDMAQGVRTV LRLIQRPTEL
310 320 330 340 350
CVYWTVNYNF EDETVRNILL HQLRSQRPVI LDPTDPTNNV GKDDGFWELL
360 370 380 390 400
TEEAMAWLYS PSLNTESPAP YWDVLPMPLF VTPSHLLNKF IKDFLQPNKL
410 420 430 440 450
FLKQIKEAVD IICSFLKNVC FLNSDTKVLK TVKGGSTAKG TALKRGSDAD
460 470 480 490 500
IVVFLSSLES YDSLKTNRSQ FVQEIQKQLE EFVQAQEWEV TFEISKWKAP
510 520 530 540 550
RVLSFTLKSK TLNESVEFDV LPAYDALGQL RSDFTLRPEA YKDLIELCAS
560 570 580 590 600
QDIKEGEFSI CFTELQRNFI QTRPTKLKSL LRLIKHWYKQ YERKMKPKAS
610 620 630 640 650
LPPKYALELL TVYAWEQGSG TDDFDIAEGF RTVLDLVIKY RQLCIFWTVN
660 670 680 690 700
YNFEEEYMRK FLLTQIQKKR PVILDPADPT GDVGGGDRWC WHLLAEEAKE
710 720 730 740
WLSSPCFQVE QKGLVQPWKV PVMQTPGSCG GQIYPTVGGV TK
Length:742
Mass (Da):85,051
Last modified:April 5, 2011 - 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:iF8F21FB4BEF90C58
GO
Isoform 2 (identifier: E9Q9A9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     723-742: MQTPGSCGGQIYPTVGGVTK → PRDLKTSDMVGVFTTGGILWQDQGFLSFV

Show »
Length:751
Mass (Da):86,285
Checksum:iB4E650AE78280C49
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F7CFL3F7CFL3_MOUSE
2'-5'-oligoadenylate synthase 2
Oas2
236Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti270Y → C in BAB84135 (PubMed:12396720).Curated1
Sequence conflicti630F → L in BAB84135 (PubMed:12396720).Curated1

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 varianti232Q → R in strain: C3H/He. 2 Publications1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_044068723 – 742MQTPG…GGVTK → PRDLKTSDMVGVFTTGGILW QDQGFLSFV in isoform 2. 1 PublicationAdd BLAST20

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
AB067535 mRNA Translation: BAB84135.1
AF418010 mRNA Translation: AAM54499.1
AC115937 Genomic DNA No translation available.
CH466529 Genomic DNA Translation: EDL19753.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS19625.2 [E9Q9A9-1]
CCDS84949.1 [E9Q9A9-2]

NCBI Reference Sequences

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RefSeqi
NP_001334377.1, NM_001347448.1 [E9Q9A9-2]
NP_660262.2, NM_145227.3 [E9Q9A9-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000053909; ENSMUSP00000060082; ENSMUSG00000032690 [E9Q9A9-1]
ENSMUST00000081491; ENSMUSP00000080209; ENSMUSG00000032690 [E9Q9A9-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
246728

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:246728

UCSC genome browser

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UCSCi
uc008zhw.2, mouse [E9Q9A9-2]
uc008zhx.2, mouse [E9Q9A9-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AB067535 mRNA Translation: BAB84135.1
AF418010 mRNA Translation: AAM54499.1
AC115937 Genomic DNA No translation available.
CH466529 Genomic DNA Translation: EDL19753.1
CCDSiCCDS19625.2 [E9Q9A9-1]
CCDS84949.1 [E9Q9A9-2]
RefSeqiNP_001334377.1, NM_001347448.1 [E9Q9A9-2]
NP_660262.2, NM_145227.3 [E9Q9A9-1]

3D structure databases

SMRiE9Q9A9
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi232936, 10 interactors
STRINGi10090.ENSMUSP00000060082

PTM databases

iPTMnetiE9Q9A9
PhosphoSitePlusiE9Q9A9
SwissPalmiE9Q9A9

Proteomic databases

EPDiE9Q9A9
jPOSTiE9Q9A9
MaxQBiE9Q9A9
PaxDbiE9Q9A9
PeptideAtlasiE9Q9A9
PRIDEiE9Q9A9
ProteomicsDBi289956 [E9Q9A9-1]
289957 [E9Q9A9-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
31214, 416 antibodies

The DNASU plasmid repository

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DNASUi
246728

Genome annotation databases

EnsembliENSMUST00000053909; ENSMUSP00000060082; ENSMUSG00000032690 [E9Q9A9-1]
ENSMUST00000081491; ENSMUSP00000080209; ENSMUSG00000032690 [E9Q9A9-2]
GeneIDi246728
KEGGimmu:246728
UCSCiuc008zhw.2, mouse [E9Q9A9-2]
uc008zhx.2, mouse [E9Q9A9-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4939
MGIiMGI:2180852, Oas2
VEuPathDBiHostDB:ENSMUSG00000032690

Phylogenomic databases

eggNOGiENOG502S649, Eukaryota
GeneTreeiENSGT00510000046406
HOGENOMiCLU_026275_0_0_1
InParanoidiE9Q9A9
OMAiWMKDSFE
OrthoDBi611234at2759
TreeFamiTF329749

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
246728, 3 hits in 61 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Oas2, mouse

Protein Ontology

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PROi
PR:E9Q9A9
RNActiE9Q9A9, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000032690, Expressed in bone marrow macrophage and 148 other tissues
GenevisibleiE9Q9A9, MM

Family and domain databases

CDDicd05400, NT_2-5OAS_ClassI-CCAase, 2 hits
Gene3Di3.30.460.10, 2 hits
InterProiView protein in InterPro
IPR018952, 2-5-oligoAdlate_synth_1_dom2/C
IPR026774, 2-5A_synthase
IPR006117, 2-5OAS_C_CS
IPR043518, 2-5OAS_N_CS
IPR006116, NT_2-5OAS_ClassI-CCAase
IPR043519, NT_sf
IPR002934, Polymerase_NTP_transf_dom
PANTHERiPTHR11258, PTHR11258, 1 hit
PfamiView protein in Pfam
PF01909, NTP_transf_2, 1 hit
PF10421, OAS1_C, 2 hits
SUPFAMiSSF81301, SSF81301, 2 hits
PROSITEiView protein in PROSITE
PS00832, 25A_SYNTH_1, 1 hit
PS00833, 25A_SYNTH_2, 2 hits
PS50152, 25A_SYNTH_3, 2 hits

MobiDB: a database of protein disorder and mobility annotations

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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 nameiOAS2_MOUSE
<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: E9Q9A9
Secondary accession number(s): Q8K4E5, Q8VI92
<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: September 5, 2012
Last sequence update: April 5, 2011
Last modified: September 29, 2021
This is version 78 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 programChordata 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

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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