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Q9Y6K5

- OAS3_HUMAN

UniProt

Q9Y6K5 - OAS3_HUMAN

Protein

2'-5'-oligoadenylate synthase 3

Gene

OAS3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      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 preferentially dimers 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. Displays antiviral activity against Chikungunya virus (CHIKV), Dengue virus, Sindbis virus (SINV) and Semliki forest virus (SFV).3 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium.Curated

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi816 – 8161Magnesium; catalyticSequence Analysis
    Metal bindingi818 – 8181Magnesium; catalyticSequence Analysis
    Metal bindingi888 – 8881Magnesium; catalyticSequence Analysis
    Binding sitei947 – 9471SubstrateBy similarity
    Binding sitei950 – 9501ATPBy similarity

    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

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. defense response to virus Source: UniProtKB
    3. interferon-gamma-mediated signaling pathway Source: Reactome
    4. negative regulation of viral genome replication Source: UniProtKB
    5. nucleobase-containing compound metabolic process Source: ProtInc
    6. regulation of ribonuclease activity Source: UniProtKB
    7. response to virus Source: UniProtKB
    8. 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:ENSG00000111331-MONOMER.
    ReactomeiREACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2'-5'-oligoadenylate synthase 3 (EC:2.7.7.84)
    Short name:
    (2-5')oligo(A) synthase 3
    Short name:
    2-5A synthase 3
    Alternative name(s):
    p100 OAS
    Short name:
    p100OAS
    Gene namesi
    Name:OAS3
    ORF Names:P/OKcl.4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:8088. OAS3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular space Source: UniProt
    4. intracellular membrane-bounded organelle Source: ProtInc
    5. nucleus Source: HPA
    6. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31877.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 108710872'-5'-oligoadenylate synthase 3PRO_0000160265Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9Y6K5.
    PaxDbiQ9Y6K5.
    PRIDEiQ9Y6K5.

    PTM databases

    PhosphoSiteiQ9Y6K5.

    Expressioni

    Tissue specificityi

    Present at high level in placenta trophoblast.

    Inductioni

    By type I interferon (IFN) and viruses.

    Gene expression databases

    ArrayExpressiQ9Y6K5.
    BgeeiQ9Y6K5.
    CleanExiHS_OAS3.
    GenevestigatoriQ9Y6K5.

    Organism-specific databases

    HPAiHPA041253.
    HPA041372.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DHX30Q7L2E32EBI-6115729,EBI-1211456
    EIF6P565372EBI-6115729,EBI-372243
    FTSJ3Q8IY812EBI-6115729,EBI-744088
    IFRD2Q128942EBI-6115729,EBI-6115935
    MAVSQ7Z4342EBI-6115729,EBI-995373

    Protein-protein interaction databases

    BioGridi110994. 15 interactions.
    IntActiQ9Y6K5. 13 interactions.
    MINTiMINT-4991875.
    STRINGi9606.ENSP00000228928.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y6K5.
    SMRiQ9Y6K5. Positions 407-740, 747-1081.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni6 – 343338OAS domain 1Add
    BLAST
    Regioni344 – 41067LinkerAdd
    BLAST
    Regioni411 – 742332OAS domain 2Add
    BLAST
    Regioni750 – 1084335OAS domain 3Add
    BLAST

    Sequence similaritiesi

    Belongs to the 2-5A synthase family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG124087.
    HOGENOMiHOG000013200.
    HOVERGENiHBG007856.
    InParanoidiQ9Y6K5.
    KOiK14216.
    OMAiCQGGEHA.
    OrthoDBiEOG7WDN1R.
    PhylomeDBiQ9Y6K5.
    TreeFamiTF329749.

    Family and domain databases

    Gene3Di1.10.1410.20. 3 hits.
    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. 3 hits.
    [Graphical view]
    PROSITEiPS00832. 25A_SYNTH_1. 3 hits.
    PS00833. 25A_SYNTH_2. 2 hits.
    PS50152. 25A_SYNTH_3. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y6K5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLYSTPAAA LDRFVARRLQ PRKEFVEKAR RALGALAAAL RERGGRLGAA     50
    APRVLKTVKG GSSGRGTALK GGCDSELVIF LDCFKSYVDQ RARRAEILSE 100
    MRASLESWWQ NPVPGLRLTF PEQSVPGALQ FRLTSVDLED WMDVSLVPAF 150
    NVLGQAGSGV KPKPQVYSTL LNSGCQGGEH AACFTELRRN FVNIRPAKLK 200
    NLILLVKHWY HQVCLQGLWK ETLPPVYALE LLTIFAWEQG CKKDAFSLAE 250
    GLRTVLGLIQ QHQHLCVFWT VNYGFEDPAV GQFLQRQLKR PRPVILDPAD 300
    PTWDLGNGAA WHWDLLAQEA ASCYDHPCFL RGMGDPVQSW KGPGLPRAGC 350
    SGLGHPIQLD PNQKTPENSK SLNAVYPRAG SKPPSCPAPG PTGAASIVPS 400
    VPGMALDLSQ IPTKELDRFI QDHLKPSPQF QEQVKKAIDI ILRCLHENCV 450
    HKASRVSKGG SFGRGTDLRD GCDVELIIFL NCFTDYKDQG PRRAEILDEM 500
    RAQLESWWQD QVPSLSLQFP EQNVPEALQF QLVSTALKSW TDVSLLPAFD 550
    AVGQLSSGTK PNPQVYSRLL TSGCQEGEHK ACFAELRRNF MNIRPVKLKN 600
    LILLVKHWYR QVAAQNKGKG PAPASLPPAY ALELLTIFAW EQGCRQDCFN 650
    MAQGFRTVLG LVQQHQQLCV YWTVNYSTED PAMRMHLLGQ LRKPRPLVLD 700
    PADPTWNVGH GSWELLAQEA AALGMQACFL SRDGTSVQPW DVMPALLYQT 750
    PAGDLDKFIS EFLQPNRQFL AQVNKAVDTI CSFLKENCFR NSPIKVIKVV 800
    KGGSSAKGTA LRGRSDADLV VFLSCFSQFT EQGNKRAEII SEIRAQLEAC 850
    QQERQFEVKF EVSKWENPRV LSFSLTSQTM LDQSVDFDVL PAFDALGQLV 900
    SGSRPSSQVY VDLIHSYSNA GEYSTCFTEL QRDFIISRPT KLKSLIRLVK 950
    HWYQQCTKIS KGRGSLPPQH GLELLTVYAW EQGGKDSQFN MAEGFRTVLE 1000
    LVTQYRQLCI YWTINYNAKD KTVGDFLKQQ LQKPRPIILD PADPTGNLGH 1050
    NARWDLLAKE AAACTSALCC MGRNGIPIQP WPVKAAV 1087
    Length:1,087
    Mass (Da):121,170
    Last modified:January 11, 2011 - v3
    Checksum:i36DAADE4574DE961
    GO

    Sequence cautioni

    The sequence AAD28543.1 differs from that shown. Reason: Frameshift at positions 394 and 398.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti159 – 1591G → A in AAD28543. (PubMed:9880533)Curated
    Sequence conflicti249 – 2491A → G in AAD28543. (PubMed:9880533)Curated
    Sequence conflicti287 – 2882QL → HV in AAD28543. (PubMed:9880533)Curated
    Sequence conflicti316 – 3161L → H in AAD28543. (PubMed:9880533)Curated
    Sequence conflicti393 – 3931G → A in AAD28543. (PubMed:9880533)Curated
    Sequence conflicti503 – 5042QL → HV in AAD28543. (PubMed:9880533)Curated
    Sequence conflicti503 – 5042QL → HV in BAB18647. (PubMed:11280764)Curated
    Sequence conflicti984 – 9841G → R in BAB18647. (PubMed:11280764)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181R → K.1 Publication
    Corresponds to variant rs1859330 [ dbSNP | Ensembl ].
    VAR_060076
    Natural varianti18 – 181R → M.
    Corresponds to variant rs1859330 [ dbSNP | Ensembl ].
    VAR_060077
    Natural varianti18 – 181R → T.
    Corresponds to variant rs1859330 [ dbSNP | Ensembl ].
    VAR_060078
    Natural varianti65 – 651R → W.
    Corresponds to variant rs12819767 [ dbSNP | Ensembl ].
    VAR_057660
    Natural varianti378 – 3781R → K.
    Corresponds to variant rs45519442 [ dbSNP | Ensembl ].
    VAR_062127
    Natural varianti381 – 3811S → R.1 Publication
    Corresponds to variant rs2285933 [ dbSNP | Ensembl ].
    VAR_057661
    Natural varianti869 – 8691R → H.
    Corresponds to variant rs16942374 [ dbSNP | Ensembl ].
    VAR_057662

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF063613 mRNA. Translation: AAD28543.1. Frameshift.
    AB044545 mRNA. Translation: BAB18647.1.
    AC004551 Genomic DNA. No translation available.
    BC113746 mRNA. Translation: AAI13747.1.
    AF251351 Genomic DNA. No translation available.
    CCDSiCCDS44981.1.
    RefSeqiNP_006178.2. NM_006187.2.
    UniGeneiHs.528634.
    Hs.744211.

    Genome annotation databases

    EnsembliENST00000228928; ENSP00000228928; ENSG00000111331.
    GeneIDi4940.
    KEGGihsa:4940.
    UCSCiuc001tug.3. human.

    Polymorphism databases

    DMDMi317373408.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF063613 mRNA. Translation: AAD28543.1 . Frameshift.
    AB044545 mRNA. Translation: BAB18647.1 .
    AC004551 Genomic DNA. No translation available.
    BC113746 mRNA. Translation: AAI13747.1 .
    AF251351 Genomic DNA. No translation available.
    CCDSi CCDS44981.1.
    RefSeqi NP_006178.2. NM_006187.2.
    UniGenei Hs.528634.
    Hs.744211.

    3D structure databases

    ProteinModelPortali Q9Y6K5.
    SMRi Q9Y6K5. Positions 407-740, 747-1081.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110994. 15 interactions.
    IntActi Q9Y6K5. 13 interactions.
    MINTi MINT-4991875.
    STRINGi 9606.ENSP00000228928.

    PTM databases

    PhosphoSitei Q9Y6K5.

    Polymorphism databases

    DMDMi 317373408.

    Proteomic databases

    MaxQBi Q9Y6K5.
    PaxDbi Q9Y6K5.
    PRIDEi Q9Y6K5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000228928 ; ENSP00000228928 ; ENSG00000111331 .
    GeneIDi 4940.
    KEGGi hsa:4940.
    UCSCi uc001tug.3. human.

    Organism-specific databases

    CTDi 4940.
    GeneCardsi GC12P113376.
    H-InvDB HIX0201822.
    HGNCi HGNC:8088. OAS3.
    HPAi HPA041253.
    HPA041372.
    MIMi 603351. gene.
    neXtProti NX_Q9Y6K5.
    PharmGKBi PA31877.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG124087.
    HOGENOMi HOG000013200.
    HOVERGENi HBG007856.
    InParanoidi Q9Y6K5.
    KOi K14216.
    OMAi CQGGEHA.
    OrthoDBi EOG7WDN1R.
    PhylomeDBi Q9Y6K5.
    TreeFami TF329749.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000111331-MONOMER.
    Reactomei REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.

    Miscellaneous databases

    ChiTaRSi OAS3. human.
    GeneWikii OAS3.
    GenomeRNAii 4940.
    NextBioi 19035.
    PROi Q9Y6K5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6K5.
    Bgeei Q9Y6K5.
    CleanExi HS_OAS3.
    Genevestigatori Q9Y6K5.

    Family and domain databases

    Gene3Di 1.10.1410.20. 3 hits.
    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. 3 hits.
    [Graphical view ]
    PROSITEi PS00832. 25A_SYNTH_1. 3 hits.
    PS00833. 25A_SYNTH_2. 2 hits.
    PS50152. 25A_SYNTH_3. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The 100-kDa 2',5'-oligoadenylate synthetase catalyzing preferentially the synthesis of dimeric pppA2'p5'A molecules is composed of three homologous domains."
      Rebouillat D., Hovnanian A., Marie I., Hovanessian A.G.
      J. Biol. Chem. 274:1557-1565(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
    2. "Molecular basis of T cell-mediated recognition of pancreatic cancer cells."
      Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N., Itoh K.
      Cancer Res. 61:2038-2046(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-18.
      Tissue: Pancreatic cancer.
    3. "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].
    4. "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], VARIANT ARG-381.
      Tissue: Brain.
    5. "Characterization of the gene encoding the 100-kDa form of human 2', 5'oligoadenylate synthetase."
      Rebouillat D., Hovnanian A., David G., Hovanessian A.G., Williams B.R.
      Genomics 70:232-240(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
      Tissue: Monocyte.
    6. Bienvenut W.V., Gao M., Leug H.
      Submitted (JUN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-17; 118-132; 244-253 AND 371-378, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Prostatic carcinoma.
    7. "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.
    8. "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.
    9. "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.
    10. "The large form of human 2',5'-Oligoadenylate Synthetase (OAS3) exerts antiviral effect against Chikungunya virus."
      Brehin A.C., Casademont I., Frenkiel M.P., Julier C., Sakuntabhai A., Despres P.
      Virology 384:216-222(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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.
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiOAS3_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6K5
    Secondary accession number(s): Q2HJ14, Q9H3P5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 119 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3