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P29728

- OAS2_HUMAN

UniProt

P29728 - OAS2_HUMAN

Protein

2'-5'-oligoadenylate synthase 2

Gene

OAS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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.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.1 Publication

    Kineticsi

    1. KM=2.1 mM for ATP3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi408 – 4081Magnesium; catalyticSequence Analysis
    Metal bindingi410 – 4101Magnesium; catalyticSequence Analysis
    Metal bindingi481 – 4811Magnesium; catalyticSequence Analysis
    Binding sitei544 – 5441Substrate
    Binding sitei547 – 5471ATP

    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. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. defense response to virus Source: UniProtKB-KW
    3. interferon-gamma-mediated signaling pathway Source: Reactome
    4. nucleobase-containing compound metabolic process Source: ProtInc
    5. protein glycosylation Source: UniProtKB
    6. protein myristoylation Source: UniProtKB
    7. purine nucleotide biosynthetic process Source: UniProtKB
    8. response to virus Source: UniProtKB
    9. RNA catabolic process Source: Ensembl
    10. 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:ENSG00000111335-MONOMER.
    ReactomeiREACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2'-5'-oligoadenylate synthase 2 (EC:2.7.7.84)
    Short name:
    (2-5')oligo(A) synthase 2
    Short name:
    2-5A synthase 2
    Alternative name(s):
    p69 OAS / p71 OAS
    Short name:
    p69OAS / p71OAS
    Gene namesi
    Name:OAS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:8087. OAS2.

    Subcellular locationi

    Cytoplasm. Cytoplasmperinuclear region. Mitochondrion. Nucleus. Microsome. Endoplasmic reticulum
    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. intracellular membrane-bounded organelle Source: ProtInc
    5. membrane Source: UniProtKB
    6. mitochondrion Source: UniProtKB-SubCell
    7. nucleus Source: UniProtKB-SubCell
    8. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A or D: No loss of activity. 1 Publication
    Mutagenesisi408 – 4081D → A: Loss of activity; when associated with A-410. 1 Publication
    Mutagenesisi410 – 4101D → A: Loss of activity; when associated with A-408. 1 Publication
    Mutagenesisi421 – 4211Y → P or A: Significant loss of activity. 1 Publication
    Mutagenesisi481 – 4811D → A: Loss of activity. 1 Publication
    Mutagenesisi544 – 5441R → A or Y: Significant loss of activity. 1 Publication
    Mutagenesisi547 – 5471K → A: Partial loss of activity. 1 Publication
    Mutagenesisi668 – 6681C → A: Loss of activity; when associated with A-669 and A-670. 1 Publication
    Mutagenesisi669 – 6691F → A: Loss of activity; when associated with A-668 and A-670. 1 Publication
    Mutagenesisi670 – 6701K → A: Loss of activity; when associated with A-668 and A-669. 1 Publication

    Organism-specific databases

    PharmGKBiPA31876.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 7197182'-5'-oligoadenylate synthase 2PRO_0000160264Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine2 Publications
    Modified residuei378 – 3781N6-acetyllysine1 Publication

    Post-translational modificationi

    Myristoylation is not essential for its activity.2 Publications
    Glycosylated. Glycosylation is essential for its activity.1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Lipoprotein, Myristate

    Proteomic databases

    MaxQBiP29728.
    PaxDbiP29728.
    PRIDEiP29728.

    PTM databases

    PhosphoSiteiP29728.

    Expressioni

    Inductioni

    By type I interferon (IFN) and viruses.

    Gene expression databases

    ArrayExpressiP29728.
    BgeeiP29728.
    CleanExiHS_OAS2.
    GenevestigatoriP29728.

    Organism-specific databases

    HPAiCAB024984.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi110993. 2 interactions.
    STRINGi9606.ENSP00000342278.

    Structurei

    3D structure databases

    ProteinModelPortaliP29728.
    SMRiP29728. Positions 7-336, 340-680.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 335325OAS domain 1Add
    BLAST
    Regioni343 – 683341OAS domain 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi326 – 34621Pro-rich (linker)Add
    BLAST

    Sequence similaritiesi

    Belongs to the 2-5A synthase family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG124087.
    HOGENOMiHOG000013200.
    HOVERGENiHBG007855.
    InParanoidiP29728.
    KOiK14216.
    OMAiKSYTSQK.
    OrthoDBiEOG7WDN1R.
    PhylomeDBiP29728.
    TreeFamiTF329749.

    Family and domain databases

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

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform p71 (identifier: P29728-1) [UniParc]FASTAAdd to Basket

    Also known as: 71 kDa

    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

    MGNGESQLSS VPAQKLGWFI QEYLKPYEEC QTLIDEMVNT ICDVLQEPEQ    50
    FPLVQGVAIG GSYGRKTVLR GNSDGTLVLF FSDLKQFQDQ KRSQRDILDK 100
    TGDKLKFCLF TKWLKNNFEI QKSLDGFTIQ VFTKNQRISF EVLAAFNALS 150
    LNDNPSPWIY RELKRSLDKT NASPGEFAVC FTELQQKFFD NRPGKLKDLI 200
    LLIKHWHQQC QKKIKDLPSL SPYALELLTV YAWEQGCRKD NFDIAEGVRT 250
    VLELIKCQEK LCIYWMVNYN FEDETIRNIL LHQLQSARPV ILDPVDPTNN 300
    VSGDKICWQW LKKEAQTWLT SPNLDNELPA PSWNVLPAPL FTTPGHLLDK 350
    FIKEFLQPNK CFLEQIDSAV NIIRTFLKEN CFRQSTAKIQ IVRGGSTAKG 400
    TALKTGSDAD LVVFHNSLKS YTSQKNERHK IVKEIHEQLK AFWREKEEEL 450
    EVSFEPPKWK APRVLSFSLK SKVLNESVSF DVLPAFNALG QLSSGSTPSP 500
    EVYAGLIDLY KSSDLPGGEF STCFTVLQRN FIRSRPTKLK DLIRLVKHWY 550
    KECERKLKPK GSLPPKYALE LLTIYAWEQG SGVPDFDTAE GFRTVLELVT 600
    QYQQLCIFWK VNYNFEDETV RKFLLSQLQK TRPVILDPAE PTGDVGGGDR 650
    WCWHLLAKEA KEWLSSPCFK DGTGNPIPPW KVPTMQTPGS CGARIHPIVN 700
    EMFSSRSHRI LNNNSKRNF 719
    Length:719
    Mass (Da):82,431
    Last modified:January 23, 2007 - v3
    Checksum:i1B680D397D5EDB78
    GO
    Isoform p69 (identifier: P29728-2) [UniParc]FASTAAdd to Basket

    Also known as: 69 kDa

    The sequence of this isoform differs from the canonical sequence as follows:
         684-687: TMQT → VKVI
         688-719: Missing.

    Show »
    Length:687
    Mass (Da):78,787
    Checksum:i34729B5A88A38B2D
    GO
    Isoform 3 (identifier: P29728-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         151-172: LNDNPSPWIYRELKRSLDKTNA → KHCWVSGEKSQRSGCQTALCNL
         173-719: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:172
    Mass (Da):19,517
    Checksum:i8CF5C0C9EE9850A9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 473LQE → CRN in AAA60607. (PubMed:1577824)Curated
    Sequence conflicti45 – 473LQE → CRN in AAA60606. (PubMed:1577824)Curated
    Sequence conflicti127 – 1271F → S in AAA60607. (PubMed:1577824)Curated
    Sequence conflicti127 – 1271F → S in AAA60606. (PubMed:1577824)Curated
    Sequence conflicti606 – 6061C → G in AAA60607. (PubMed:1577824)Curated
    Sequence conflicti606 – 6061C → G in AAA60606. (PubMed:1577824)Curated
    Sequence conflicti639 – 6391A → G in AAA60607. (PubMed:1577824)Curated
    Sequence conflicti639 – 6391A → G in AAA60606. (PubMed:1577824)Curated
    Sequence conflicti657 – 6571A → D in AAA60607. (PubMed:1577824)Curated
    Sequence conflicti657 – 6571A → D in AAA60606. (PubMed:1577824)Curated
    Sequence conflicti662 – 6632EW → VR in AAA60607. (PubMed:1577824)Curated
    Sequence conflicti662 – 6632EW → VR in AAA60606. (PubMed:1577824)Curated
    Sequence conflicti719 – 7191F → FWRSSGNRF in AAA60607. (PubMed:1577824)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei151 – 17222LNDNP…DKTNA → KHCWVSGEKSQRSGCQTALC NL in isoform 3. 1 PublicationVSP_043354Add
    BLAST
    Alternative sequencei173 – 719547Missing in isoform 3. 1 PublicationVSP_043355Add
    BLAST
    Alternative sequencei684 – 6874TMQT → VKVI in isoform p69. 3 PublicationsVSP_003741
    Alternative sequencei688 – 71932Missing in isoform p69. 3 PublicationsVSP_003742Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87434 mRNA. Translation: AAA60607.1.
    M87284 mRNA. Translation: AAA60606.1.
    AK292796 mRNA. Translation: BAF85485.1.
    AC004551 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW98027.1.
    BC023637 mRNA. Translation: AAH23637.1.
    BC049215 mRNA. Translation: AAH49215.1.
    CCDSiCCDS31906.1. [P29728-1]
    CCDS41839.1. [P29728-2]
    CCDS44982.1. [P29728-3]
    PIRiB42665.
    RefSeqiNP_001027903.1. NM_001032731.1. [P29728-3]
    NP_002526.2. NM_002535.2. [P29728-2]
    NP_058197.2. NM_016817.2. [P29728-1]
    UniGeneiHs.414332.

    Genome annotation databases

    EnsembliENST00000342315; ENSP00000342278; ENSG00000111335. [P29728-1]
    ENST00000392583; ENSP00000376362; ENSG00000111335. [P29728-2]
    ENST00000449768; ENSP00000411763; ENSG00000111335. [P29728-3]
    GeneIDi4939.
    KEGGihsa:4939.
    UCSCiuc001tuh.3. human. [P29728-3]
    uc001tui.1. human. [P29728-2]
    uc001tuj.3. human. [P29728-1]

    Polymorphism databases

    DMDMi116242687.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87434 mRNA. Translation: AAA60607.1 .
    M87284 mRNA. Translation: AAA60606.1 .
    AK292796 mRNA. Translation: BAF85485.1 .
    AC004551 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW98027.1 .
    BC023637 mRNA. Translation: AAH23637.1 .
    BC049215 mRNA. Translation: AAH49215.1 .
    CCDSi CCDS31906.1. [P29728-1 ]
    CCDS41839.1. [P29728-2 ]
    CCDS44982.1. [P29728-3 ]
    PIRi B42665.
    RefSeqi NP_001027903.1. NM_001032731.1. [P29728-3 ]
    NP_002526.2. NM_002535.2. [P29728-2 ]
    NP_058197.2. NM_016817.2. [P29728-1 ]
    UniGenei Hs.414332.

    3D structure databases

    ProteinModelPortali P29728.
    SMRi P29728. Positions 7-336, 340-680.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110993. 2 interactions.
    STRINGi 9606.ENSP00000342278.

    PTM databases

    PhosphoSitei P29728.

    Polymorphism databases

    DMDMi 116242687.

    Proteomic databases

    MaxQBi P29728.
    PaxDbi P29728.
    PRIDEi P29728.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342315 ; ENSP00000342278 ; ENSG00000111335 . [P29728-1 ]
    ENST00000392583 ; ENSP00000376362 ; ENSG00000111335 . [P29728-2 ]
    ENST00000449768 ; ENSP00000411763 ; ENSG00000111335 . [P29728-3 ]
    GeneIDi 4939.
    KEGGi hsa:4939.
    UCSCi uc001tuh.3. human. [P29728-3 ]
    uc001tui.1. human. [P29728-2 ]
    uc001tuj.3. human. [P29728-1 ]

    Organism-specific databases

    CTDi 4939.
    GeneCardsi GC12P113416.
    H-InvDB HIX0129679.
    HGNCi HGNC:8087. OAS2.
    HPAi CAB024984.
    MIMi 603350. gene.
    neXtProti NX_P29728.
    PharmGKBi PA31876.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG124087.
    HOGENOMi HOG000013200.
    HOVERGENi HBG007855.
    InParanoidi P29728.
    KOi K14216.
    OMAi KSYTSQK.
    OrthoDBi EOG7WDN1R.
    PhylomeDBi P29728.
    TreeFami TF329749.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000111335-MONOMER.
    Reactomei REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.

    Miscellaneous databases

    GeneWikii OAS2.
    GenomeRNAii 4939.
    NextBioi 19027.
    PROi P29728.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29728.
    Bgeei P29728.
    CleanExi HS_OAS2.
    Genevestigatori P29728.

    Family and domain databases

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

    Publicationsi

    1. "The 69-kDa 2-5A synthetase is composed of two homologous and adjacent functional domains."
      Marie I., Hovanessian A.G.
      J. Biol. Chem. 267:9933-9939(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P69 AND P71).
    2. "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 P69).
      Tissue: Trachea.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS P69 AND 3).
      Tissue: Blood and Uterus.
    6. "Identification of the substrate-binding sites of 2'-5'-oligoadenylate synthetase."
      Sarkar S.N., Miyagi M., Crabb J.W., Sen G.C.
      J. Biol. Chem. 277:24321-24330(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 420-425 AND 539-547, IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-421; ARG-544 AND LYS-547.
    7. "Differential expression and distinct structure of 69- and 100-kDa forms of 2-5A synthetase in human cells treated with interferon."
      Marie I., Svab J., Robert N., Galabru J., Hovanessian A.G.
      J. Biol. Chem. 265:18601-18607(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION.
    8. "Enzymatic characteristics of recombinant medium isozyme of 2'-5' oligoadenylate synthetase."
      Sarkar S.N., Bandyopadhyay S., Ghosh A., Sen G.C.
      J. Biol. Chem. 274:1848-1855(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION, GLYCOSYLATION, MYRISTOYLATION, MUTAGENESIS OF GLY-2.
    9. "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: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-408; ASP-410; ASP-481; CYS-668; PHE-669 AND LYS-670.
    10. "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.
    11. "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.
    12. "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.
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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.

    Entry informationi

    Entry nameiOAS2_HUMAN
    AccessioniPrimary (citable) accession number: P29728
    Secondary accession number(s): A8K9T1, Q6PJ33, Q86XX8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 135 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3