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P00973

- OAS1_HUMAN

UniProt

P00973 - OAS1_HUMAN

Protein

2'-5'-oligoadenylate synthase 1

Gene

OAS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 4 (18 May 2010)
      Previous versions | rss
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    Functioni

    Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L.4 Publications

    Catalytic activityi

    3 ATP = pppA2'p5'A2'p5'A + 2 diphosphate.2 Publications

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    Produced as a latent enzyme which is activated by dsRNA generated during the course of viral infection. The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated. ssRNA or dsDNA do not act as activators.2 Publications

    Kineticsi

    1. KM=0.31 mM for ATP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei63 – 631ATP1 Publication
    Metal bindingi75 – 751Magnesium; catalytic
    Metal bindingi77 – 771Magnesium; catalytic
    Metal bindingi148 – 1481Magnesium; catalytic
    Sitei158 – 1581Interaction with dsRNA
    Binding sitei213 – 2131ATP1 Publication
    Binding sitei229 – 2291ATP1 Publication

    GO - Molecular functioni

    1. 2'-5'-oligoadenylate synthetase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB
    3. double-stranded RNA binding Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: IntAct
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to interferon-alpha Source: UniProtKB
    2. cytokine-mediated signaling pathway Source: Reactome
    3. defense response to virus Source: UniProtKB
    4. glucose homeostasis Source: UniProt
    5. glucose metabolic process Source: UniProt
    6. interferon-gamma-mediated signaling pathway Source: Reactome
    7. negative regulation of viral genome replication Source: UniProtKB
    8. protein oligomerization Source: UniProtKB
    9. purine nucleotide biosynthetic process Source: UniProtKB
    10. regulation of ribonuclease activity Source: UniProtKB
    11. response to virus Source: UniProtKB
    12. type I interferon signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Antiviral defense, Immunity, Innate immunity

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000089127-MONOMER.
    ReactomeiREACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2'-5'-oligoadenylate synthase 1 (EC:2.7.7.84)
    Short name:
    (2-5')oligo(A) synthase 1
    Short name:
    2-5A synthase 1
    Alternative name(s):
    E18/E16
    p46/p42 OAS
    Gene namesi
    Name:OAS1
    Synonyms:OIAS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:8086. OAS1.

    Subcellular locationi

    Cytoplasm 1 Publication. Mitochondrion 1 Publication. Nucleus 1 Publication. Microsome 1 Publication. Endoplasmic reticulum 1 Publication. Secreted By similarity
    Note: Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. endoplasmic reticulum Source: UniProtKB-SubCell
    4. extracellular region Source: UniProtKB-SubCell
    5. mitochondrion Source: UniProtKB-SubCell
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi66 – 661K → A: Decreased enzyme activity. 1 Publication
    Mutagenesisi75 – 751D → A: Loss of activity; when associated with A-77. 1 Publication
    Mutagenesisi77 – 771D → A: Loss of activity; when associated with A-75. 1 Publication
    Mutagenesisi148 – 1481D → A: Strongly reduced enzyme activity. 1 Publication
    Mutagenesisi233 – 2331E → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi331 – 3311C → A: Loss of activity; when associated with A-332 and A-333. 1 Publication
    Mutagenesisi332 – 3321F → A: Loss of activity; when associated with A-331 and A-333. 1 Publication
    Mutagenesisi333 – 3331K → A: Loss of activity; when associated with A-331 and A-332. 1 Publication

    Organism-specific databases

    PharmGKBiPA31875.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4004002'-5'-oligoadenylate synthase 1PRO_0000160259Add
    BLAST

    Proteomic databases

    MaxQBiP00973.
    PaxDbiP00973.
    PRIDEiP00973.

    PTM databases

    PhosphoSiteiP00973.

    Expressioni

    Inductioni

    By type I interferon (IFN) and viruses.2 Publications

    Gene expression databases

    ArrayExpressiP00973.
    BgeeiP00973.
    GenevestigatoriP00973.

    Organism-specific databases

    HPAiCAB021104.
    HPA003657.

    Interactioni

    Subunit structurei

    Monomer By similarity. Homotetramer.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRMT6Q96LA82EBI-3932815,EBI-912440

    Protein-protein interaction databases

    BioGridi110992. 4 interactions.
    IntActiP00973. 3 interactions.
    MINTiMINT-7003225.

    Structurei

    Secondary structure

    1
    400
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4 – 63
    Helixi9 – 113
    Helixi12 – 198
    Helixi24 – 4320
    Turni44 – 463
    Beta strandi55 – 617
    Helixi62 – 665
    Turni71 – 733
    Beta strandi76 – 849
    Helixi88 – 11124
    Turni112 – 1143
    Beta strandi116 – 1183
    Beta strandi132 – 1376
    Turni139 – 1413
    Beta strandi145 – 1528
    Beta strandi161 – 1633
    Helixi167 – 17913
    Turni183 – 1864
    Helixi187 – 1904
    Helixi191 – 1955
    Turni196 – 2005
    Helixi203 – 22321
    Helixi229 – 24315
    Helixi251 – 26313
    Helixi265 – 2673
    Beta strandi278 – 2803
    Helixi281 – 29010
    Beta strandi293 – 2953
    Beta strandi297 – 3004
    Beta strandi303 – 3086
    Helixi313 – 32614
    Helixi330 – 3323

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IG8X-ray2.70A1-347[»]
    ProteinModelPortaliP00973.
    SMRiP00973. Positions 3-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni13 – 6048Interaction with dsRNAAdd
    BLAST
    Regioni200 – 21011Interaction with dsRNAAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-5A synthase family.Curated

    Phylogenomic databases

    eggNOGiNOG48070.
    HOVERGENiHBG000994.
    KOiK14216.
    OMAiNCKKKLG.
    OrthoDBiEOG7WDN1R.
    PhylomeDBiP00973.
    TreeFamiTF329749.

    Family and domain databases

    Gene3Di1.10.1410.20. 1 hit.
    InterProiIPR006117. 2-5-oligoadenylate_synth_CS.
    IPR006116. 2-5-oligoadenylate_synth_N.
    IPR018952. 2-5-oligoAdlate_synth_1_dom2/C.
    IPR026774. 2-5A_synthase.
    IPR002934. Nucleotidyltransferase.
    [Graphical view]
    PANTHERiPTHR11258. PTHR11258. 1 hit.
    PfamiPF01909. NTP_transf_2. 1 hit.
    PF10421. OAS1_C. 1 hit.
    [Graphical view]
    PROSITEiPS00832. 25A_SYNTH_1. 1 hit.
    PS00833. 25A_SYNTH_2. 1 hit.
    PS50152. 25A_SYNTH_3. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform p46 (identifier: P00973-1) [UniParc]FASTAAdd to Basket

    Also known as: 46 kDa, E18

    This isoform has been chosen as the 'canonical' 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

    MMDLRNTPAK SLDKFIEDYL LPDTCFRMQI NHAIDIICGF LKERCFRGSS    50
    YPVCVSKVVK GGSSGKGTTL RGRSDADLVV FLSPLTTFQD QLNRRGEFIQ 100
    EIRRQLEACQ RERAFSVKFE VQAPRWGNPR ALSFVLSSLQ LGEGVEFDVL 150
    PAFDALGQLT GGYKPNPQIY VKLIEECTDL QKEGEFSTCF TELQRDFLKQ 200
    RPTKLKSLIR LVKHWYQNCK KKLGKLPPQY ALELLTVYAW ERGSMKTHFN 250
    TAQGFRTVLE LVINYQQLCI YWTKYYDFKN PIIEKYLRRQ LTKPRPVILD 300
    PADPTGNLGG GDPKGWRQLA QEAEAWLNYP CFKNWDGSPV SSWILLAESN 350
    SADDETDDPR RYQKYGYIGT HEYPHFSHRP STLQAASTPQ AEEDWTCTIL 400
    Length:400
    Mass (Da):46,029
    Last modified:May 18, 2010 - v4
    Checksum:i03F0A3AA17DAD4E4
    GO
    Isoform p41 (identifier: P00973-2) [UniParc]FASTAAdd to Basket

    Also known as: 41 kDa, E16, 3-9

    The sequence of this isoform differs from the canonical sequence as follows:
         347-364: AESNSADDETDDPRRYQK → VRPPASSLPFIPAPLHEA
         365-400: Missing.

    Show »
    Length:364
    Mass (Da):41,740
    Checksum:i2FC9CA8944EC5901
    GO
    Isoform p48 (identifier: P00973-3) [UniParc]FASTAAdd to Basket

    Also known as: 9-2

    The sequence of this isoform differs from the canonical sequence as follows:
         347-400: AESNSADDET...AEEDWTCTIL → TQHTPGSIHP...CIIQDRTQVS

    Show »
    Length:414
    Mass (Da):47,408
    Checksum:iE17B28ECAE185399
    GO
    Isoform p44 (identifier: P00973-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         347-382: AESNSADDETDDPRRYQKYGYIGTHEYPHFSHRPST → VNLTLVGRRNYPIISEHAVNLQQTRRASLSYSFQVA
         383-400: Missing.

    Show »
    Length:382
    Mass (Da):43,944
    Checksum:i89654CF4DFFD195C
    GO

    Sequence cautioni

    The sequence AAA39857.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAA39858.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAA59955.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD96726.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA30164.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA26497.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181D → E in AAA39857. (PubMed:1651324)Curated
    Sequence conflicti111 – 1111R → S in AAH71981. (PubMed:15489334)Curated
    Sequence conflicti115 – 1151F → L in AAB59552. (PubMed:2416561)Curated
    Sequence conflicti115 – 1151F → L in AAB59553. (PubMed:2416561)Curated
    Sequence conflicti115 – 1151F → L in CAA26633. (PubMed:2416561)Curated
    Sequence conflicti120 – 1201E → V in BAD96726. 1 PublicationCurated
    Sequence conflicti122 – 1221Q → QE in AAA39858. (PubMed:1651324)Curated
    Sequence conflicti157 – 1571G → D in AAA39857. (PubMed:1651324)Curated
    Sequence conflicti176 – 1761E → D in AAA39858. (PubMed:1651324)Curated
    Sequence conflicti295 – 2951R → T in CAB51602. (PubMed:3753689)Curated
    Sequence conflicti315 – 3151G → R in CAB51602. (PubMed:3753689)Curated
    Isoform p48 (identifier: P00973-3)
    Sequence conflicti397 – 3971G → R in AAA39858. (PubMed:1651324)Curated
    Sequence conflicti397 – 3971G → R in AAW63050. (PubMed:17024523)Curated
    Sequence conflicti397 – 3971G → R in CAA26497. (PubMed:2411547)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311N → D.1 Publication
    Corresponds to variant rs1050994 [ dbSNP | Ensembl ].
    VAR_060471
    Natural varianti127 – 1271G → R.
    Corresponds to variant rs4767022 [ dbSNP | Ensembl ].
    VAR_060472
    Natural varianti162 – 1621G → S.9 Publications
    Corresponds to variant rs1131454 [ dbSNP | Ensembl ].
    VAR_034872
    Natural varianti352 – 3521A → T.3 Publications
    Corresponds to variant rs1131476 [ dbSNP | Ensembl ].
    VAR_060473
    Natural varianti354 – 3541D → G.
    Corresponds to variant rs35919998 [ dbSNP | Ensembl ].
    VAR_057658
    Natural varianti361 – 3611R → T.3 Publications
    Corresponds to variant rs1051042 [ dbSNP | Ensembl ].
    VAR_057659

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei347 – 40054AESNS…TCTIL → TQHTPGSIHPTGRRGLDLHH PLNASASWGKGLQCYLDQFL HFQVGLLIQRGQSSSVSWCI IQDRTQVS in isoform p48. 2 PublicationsVSP_003740Add
    BLAST
    Alternative sequencei347 – 38236AESNS…HRPST → VNLTLVGRRNYPIISEHAVN LQQTRRASLSYSFQVA in isoform p44. 1 PublicationVSP_027804Add
    BLAST
    Alternative sequencei347 – 36418AESNS…RRYQK → VRPPASSLPFIPAPLHEA in isoform p41. 8 PublicationsVSP_003738Add
    BLAST
    Alternative sequencei365 – 40036Missing in isoform p41. 8 PublicationsVSP_003739Add
    BLAST
    Alternative sequencei383 – 40018Missing in isoform p44. 1 PublicationVSP_027805Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11809
    , M11805, M11806, M11807, M11808 Genomic DNA. Translation: AAB59552.1.
    M11810 Genomic DNA. Translation: AAB59553.1.
    X02874 mRNA. Translation: CAA26633.1.
    X02875 mRNA. Translation: CAA26634.1.
    X04371 mRNA. Translation: CAB51602.1.
    D00068 mRNA. Translation: BAA00047.1.
    M63849 Genomic DNA. Translation: AAA39857.1. Different initiation.
    M63850 Genomic DNA. Translation: AAA39858.1. Different initiation.
    AJ629455 mRNA. Translation: CAF33358.1.
    AY730628 mRNA. Translation: AAW63050.1.
    DQ445949 Genomic DNA. Translation: ABE27977.1.
    AK291003 mRNA. Translation: BAF83692.1.
    BT006785 mRNA. Translation: AAP35431.1.
    AK223006 mRNA. Translation: BAD96726.1. Different initiation.
    AC004551 Genomic DNA. No translation available.
    BC000562 mRNA. Translation: AAH00562.4.
    BC061587 mRNA. Translation: AAH61587.1.
    BC071981 mRNA. Translation: AAH71981.3.
    X06560 Genomic DNA. Translation: CAA29803.1.
    M18099 Genomic DNA. Translation: AAA59955.1. Different initiation.
    X07179 Genomic DNA. Translation: CAA30164.1. Different initiation.
    X02661 mRNA. Translation: CAA26497.1. Sequence problems.
    CCDSiCCDS31905.1. [P00973-3]
    CCDS41838.1. [P00973-1]
    CCDS44980.1. [P00973-2]
    PIRiA39417. SYMSO2.
    A91013. SYHU16.
    B24359. SYHU18.
    B39417. SYMSO3.
    RefSeqiNP_001027581.1. NM_001032409.1. [P00973-3]
    NP_002525.2. NM_002534.2. [P00973-2]
    NP_058132.2. NM_016816.2. [P00973-1]
    UniGeneiHs.524760.

    Genome annotation databases

    EnsembliENST00000202917; ENSP00000202917; ENSG00000089127. [P00973-1]
    ENST00000445409; ENSP00000388001; ENSG00000089127. [P00973-3]
    ENST00000452357; ENSP00000415721; ENSG00000089127. [P00973-2]
    GeneIDi4938.
    KEGGihsa:4938.
    UCSCiuc001tub.3. human. [P00973-2]
    uc001tuc.3. human. [P00973-3]
    uc001tud.3. human. [P00973-1]

    Polymorphism databases

    DMDMi296439492.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11809
    , M11805 , M11806 , M11807 , M11808 Genomic DNA. Translation: AAB59552.1 .
    M11810 Genomic DNA. Translation: AAB59553.1 .
    X02874 mRNA. Translation: CAA26633.1 .
    X02875 mRNA. Translation: CAA26634.1 .
    X04371 mRNA. Translation: CAB51602.1 .
    D00068 mRNA. Translation: BAA00047.1 .
    M63849 Genomic DNA. Translation: AAA39857.1 . Different initiation.
    M63850 Genomic DNA. Translation: AAA39858.1 . Different initiation.
    AJ629455 mRNA. Translation: CAF33358.1 .
    AY730628 mRNA. Translation: AAW63050.1 .
    DQ445949 Genomic DNA. Translation: ABE27977.1 .
    AK291003 mRNA. Translation: BAF83692.1 .
    BT006785 mRNA. Translation: AAP35431.1 .
    AK223006 mRNA. Translation: BAD96726.1 . Different initiation.
    AC004551 Genomic DNA. No translation available.
    BC000562 mRNA. Translation: AAH00562.4 .
    BC061587 mRNA. Translation: AAH61587.1 .
    BC071981 mRNA. Translation: AAH71981.3 .
    X06560 Genomic DNA. Translation: CAA29803.1 .
    M18099 Genomic DNA. Translation: AAA59955.1 . Different initiation.
    X07179 Genomic DNA. Translation: CAA30164.1 . Different initiation.
    X02661 mRNA. Translation: CAA26497.1 . Sequence problems.
    CCDSi CCDS31905.1. [P00973-3 ]
    CCDS41838.1. [P00973-1 ]
    CCDS44980.1. [P00973-2 ]
    PIRi A39417. SYMSO2.
    A91013. SYHU16.
    B24359. SYHU18.
    B39417. SYMSO3.
    RefSeqi NP_001027581.1. NM_001032409.1. [P00973-3 ]
    NP_002525.2. NM_002534.2. [P00973-2 ]
    NP_058132.2. NM_016816.2. [P00973-1 ]
    UniGenei Hs.524760.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IG8 X-ray 2.70 A 1-347 [» ]
    ProteinModelPortali P00973.
    SMRi P00973. Positions 3-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110992. 4 interactions.
    IntActi P00973. 3 interactions.
    MINTi MINT-7003225.

    PTM databases

    PhosphoSitei P00973.

    Polymorphism databases

    DMDMi 296439492.

    Proteomic databases

    MaxQBi P00973.
    PaxDbi P00973.
    PRIDEi P00973.

    Protocols and materials databases

    DNASUi 4938.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000202917 ; ENSP00000202917 ; ENSG00000089127 . [P00973-1 ]
    ENST00000445409 ; ENSP00000388001 ; ENSG00000089127 . [P00973-3 ]
    ENST00000452357 ; ENSP00000415721 ; ENSG00000089127 . [P00973-2 ]
    GeneIDi 4938.
    KEGGi hsa:4938.
    UCSCi uc001tub.3. human. [P00973-2 ]
    uc001tuc.3. human. [P00973-3 ]
    uc001tud.3. human. [P00973-1 ]

    Organism-specific databases

    CTDi 4938.
    GeneCardsi GC12P113344.
    HGNCi HGNC:8086. OAS1.
    HPAi CAB021104.
    HPA003657.
    MIMi 164350. gene.
    neXtProti NX_P00973.
    PharmGKBi PA31875.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG48070.
    HOVERGENi HBG000994.
    KOi K14216.
    OMAi NCKKKLG.
    OrthoDBi EOG7WDN1R.
    PhylomeDBi P00973.
    TreeFami TF329749.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000089127-MONOMER.
    Reactomei REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.

    Miscellaneous databases

    ChiTaRSi OAS1. human.
    GeneWikii OAS1.
    GenomeRNAii 4938.
    NextBioi 19019.
    PROi P00973.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00973.
    Bgeei P00973.
    Genevestigatori P00973.

    Family and domain databases

    Gene3Di 1.10.1410.20. 1 hit.
    InterProi IPR006117. 2-5-oligoadenylate_synth_CS.
    IPR006116. 2-5-oligoadenylate_synth_N.
    IPR018952. 2-5-oligoAdlate_synth_1_dom2/C.
    IPR026774. 2-5A_synthase.
    IPR002934. Nucleotidyltransferase.
    [Graphical view ]
    PANTHERi PTHR11258. PTHR11258. 1 hit.
    Pfami PF01909. NTP_transf_2. 1 hit.
    PF10421. OAS1_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00832. 25A_SYNTH_1. 1 hit.
    PS00833. 25A_SYNTH_2. 1 hit.
    PS50152. 25A_SYNTH_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of two forms of the interferon-induced (2'-5') oligo A synthetase of human cells based on cDNAs and gene sequences."
      Benech P., Mory Y., Revel M., Chebath J.
      EMBO J. 4:2249-2256(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS P41 AND P46), VARIANTS ASP-31; SER-162; THR-352 AND THR-361.
      Tissue: Fetal blood.
    2. "Full-length sequence and expression of the 42 kDa 2-5A synthetase induced by human interferon."
      Wathelet M.G., Moutschen S., Cravador A., Dewit L., Defilippi P., Huez G.A., Content J.
      FEBS Lett. 196:113-120(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P41), VARIANT SER-162.
    3. "Structure and expression of a cloned cDNA for human (2'-5')oligoadenylate synthetase."
      Shiojiri S., Fukunaga R., Ichii Y., Sokawa Y.
      J. Biochem. 99:1455-1464(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P41), VARIANT SER-162.
    4. "Cloning, sequencing, and expression of two murine 2'-5'-oligoadenylate synthetases. Structure-function relationships."
      Ghosh S.K., Kusari J., Bandyopadhyay S.K., Samanta H., Kumar R., Sen G.C.
      J. Biol. Chem. 266:15293-15299(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS P48 AND P41), VARIANT SER-162.
    5. "OAS1p44, a splice variant of the interferon induced human 2'-5' oligoadenylate synthetase."
      Andersen J.B., Strandbygaard D.J., Larsen S.E., Justesen J.
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P44).
    6. "The mammalian 2'-5' oligoadenylate synthetase gene family: evidence for concerted evolution of paralogous Oas1 genes in Rodentia and Artiodactyla."
      Perelygin A.A., Zharkikh A.A., Scherbik S.V., Brinton M.A.
      J. Mol. Evol. 63:562-576(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P48), VARIANTS SER-162; THR-352 AND THR-361.
    7. "Susceptibility to infection by West Nile Virus: OAS1 (OAS1 2'-5' oligoadenylate synthetase gene) stop codon detected in exon 1 of a normal individual heterozygous for the gene."
      Lee M.-K., Morshed M.G., Jorgensen D.R., Hasselback P., Goh S.-H.
      Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM P46), VARIANTS THR-352 AND THR-361.
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P41), VARIANT SER-162.
    9. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P41), VARIANT SER-162.
    10. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P41), VARIANT SER-162.
      Tissue: Small intestine.
    11. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P41), VARIANT SER-162.
      Tissue: Brain and Uterus.
    13. "New inducers revealed by the promoter sequence analysis of two interferon-activated human genes."
      Wathelet M.G., Clauss I.M., Nols C.B., Content J., Huez G.A.
      Eur. J. Biochem. 169:313-321(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
    14. "Interferon-responsive regulatory elements in the promoter of the human 2',5'-oligo(A) synthetase gene."
      Benech P., Vigneron M., Peretz D., Revel M., Chebath J.
      Mol. Cell. Biol. 7:4498-4504(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
      Tissue: Liver.
    15. "Interferon-induced binding of nuclear factors to promoter elements of the 2-5A synthetase gene."
      Rutherford M.N., Hannigan G.E., Williams B.R.G.
      EMBO J. 7:751-759(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
      Tissue: Liver.
    16. "Human 2-5A synthetase: characterization of a novel cDNA and corresponding gene structure."
      Saunders M.E., Gewert D.R., Tugwell M.E., McMahon M., Williams B.R.G.
      EMBO J. 4:1761-1768(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 231-400 (ISOFORM P48), INDUCTION.
      Tissue: Lymphoblast.
    17. "Molecular cloning and sequence of partial cDNA for interferon-induced (2'-5')oligo(A) synthetase mRNA from human cells."
      Merlin G., Chebath J., Benech P., Metz R., Revel M.
      Proc. Natl. Acad. Sci. U.S.A. 80:4904-4908(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 255-364 (ISOFORM P41).
    18. "Enzymatic activity of 2'-5'-oligoadenylate synthetase is impaired by specific mutations that affect oligomerization of the protein."
      Ghosh A., Sarkar S.N., Guo W., Bandyopadhyay S., Sen G.C.
      J. Biol. Chem. 272:33220-33226(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-331; PHE-332 AND LYS-333.
    19. "The nature of the catalytic domain of 2'-5'-oligoadenylate synthetases."
      Sarkar S.N., Ghosh A., Wang H.W., Sung S.S., Sen G.C.
      J. Biol. Chem. 274:25535-25542(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-75 AND ASP-77.
    20. "Characterization of the 2'-5'-oligoadenylate synthetase ubiquitin-like family."
      Eskildsen S., Justesen J., Schierup M.H., Hartmann R.
      Nucleic Acids Res. 31:3166-3173(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    21. "The human 2'-5'oligoadenylate synthetase family: unique interferon-inducible enzymes catalyzing 2'-5' instead of 3'-5' phosphodiester bond formation."
      Hovanessian A.G., Justesen J.
      Biochimie 89:779-788(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    22. "The p59 oligoadenylate synthetase-like protein possesses antiviral activity that requires the C-terminal ubiquitin-like domain."
      Marques J., Anwar J., Eskildsen-Larsen S., Rebouillat D., Paludan S.R., Sen G., Williams B.R., Hartmann R.
      J. Gen. Virol. 89:2767-2772(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family members against dengue virus infection."
      Lin R.J., Yu H.P., Chang B.L., Tang W.C., Liao C.L., Lin Y.L.
      J. Immunol. 183:8035-8043(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    24. "Differential regulation of the OASL and OAS1 genes in response to viral infections."
      Melchjorsen J., Kristiansen H., Christiansen R., Rintahaka J., Matikainen S., Paludan S.R., Hartmann R.
      J. Interferon Cytokine Res. 29:199-207(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    25. "Evolution of the 2'-5'-oligoadenylate synthetase family in eukaryotes and bacteria."
      Kjaer K.H., Poulsen J.B., Reintamm T., Saby E., Martensen P.M., Kelve M., Justesen J.
      J. Mol. Evol. 69:612-624(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "The oligoadenylate synthetase family: an ancient protein family with multiple antiviral activities."
      Kristiansen H., Gad H.H., Eskildsen-Larsen S., Despres P., Hartmann R.
      J. Interferon Cytokine Res. 31:41-47(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    28. "Structural basis for cytosolic double-stranded RNA surveillance by human oligoadenylate synthetase 1."
      Donovan J., Dufner M., Korennykh A.
      Proc. Natl. Acad. Sci. U.S.A. 110:1652-1657(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-347 IN COMPLEX WITH DSRNA; MAGNESIUM IONS AND ATP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF LYS-66; ASP-148 AND GLU-233.

    Entry informationi

    Entry nameiOAS1_HUMAN
    AccessioniPrimary (citable) accession number: P00973
    Secondary accession number(s): A8K4N8
    , P04820, P29080, P29081, P78485, P78486, Q16700, Q16701, Q1PG42, Q3ZM01, Q53GC5, Q53YA4, Q6A1Z3, Q6IPC6, Q6P7N9, Q96J61
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 160 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    PubMed:1651324 sequence was originally thought to originate from mouse.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3