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Q15646

- OASL_HUMAN

UniProt

Q15646 - OASL_HUMAN

Protein

2'-5'-oligoadenylate synthase-like protein

Gene

OASL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. Displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L.3 Publications

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. DNA binding Source: UniProtKB
    3. double-stranded RNA binding Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. thyroid hormone receptor binding Source: UniProtKB
    6. transferase activity Source: InterPro

    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. negative regulation of viral genome replication Source: UniProtKB
    5. response to virus Source: UniProtKB
    6. type I interferon signaling pathway Source: Reactome

    Keywords - Biological processi

    Antiviral defense, Immunity, Innate immunity

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2'-5'-oligoadenylate synthase-like protein
    Alternative name(s):
    2'-5'-OAS-related protein
    Short name:
    2'-5'-OAS-RP
    59 kDa 2'-5'-oligoadenylate synthase-like protein
    Thyroid receptor-interacting protein 14
    Short name:
    TR-interacting protein 14
    Short name:
    TRIP-14
    p59 OASL
    Short name:
    p59OASL
    Gene namesi
    Name:OASL
    Synonyms:TRIP14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:8090. OASL.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB
    4. nucleolus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31879.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 5145132'-5'-oligoadenylate synthase-like proteinPRO_0000160266Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ15646.
    PaxDbiQ15646.
    PRIDEiQ15646.

    PTM databases

    PhosphoSiteiQ15646.

    Expressioni

    Tissue specificityi

    Expressed in most tissues, with the highest levels in primary blood Leukocytes and other hematopoietic system tissues, colon, stomach and to some extent in testis.

    Inductioni

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

    Gene expression databases

    BgeeiQ15646.
    CleanExiHS_OASL.
    GenevestigatoriQ15646.

    Organism-specific databases

    HPAiHPA001474.

    Interactioni

    Subunit structurei

    Specifically interacts with the ligand binding domain of the thyroid receptor (TR). TRIP14 does not require the presence of thyroid hormone for its interaction. Binds MBD1.1 Publication

    Protein-protein interaction databases

    BioGridi114191. 3 interactions.
    IntActiQ15646. 1 interaction.
    MINTiMINT-4993190.
    STRINGi9606.ENSP00000257570.

    Structurei

    Secondary structure

    1
    514
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi434 – 4407
    Turni441 – 4433
    Beta strandi444 – 4507
    Beta strandi452 – 4554
    Helixi456 – 46611
    Turni471 – 4733
    Beta strandi474 – 4785
    Beta strandi485 – 4884
    Helixi489 – 4924
    Beta strandi498 – 5047

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WH3NMR-A434-507[»]
    ProteinModelPortaliQ15646.
    SMRiQ15646. Positions 6-346, 368-514.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15646.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini354 – 43380Ubiquitin-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini434 – 50976Ubiquitin-like 2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The ubiquitin-like domains are essential for its antiviral activity.

    Sequence similaritiesi

    Belongs to the 2-5A synthase family.Curated
    Contains 2 ubiquitin-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG309765.
    HOGENOMiHOG000022614.
    HOVERGENiHBG000994.
    InParanoidiQ15646.
    KOiK14608.
    OMAiCFHSFQE.
    OrthoDBiEOG7WDN1R.
    PhylomeDBiQ15646.
    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.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PANTHERiPTHR11258. PTHR11258. 1 hit.
    PfamiPF10421. OAS1_C. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view]
    SMARTiSM00213. UBQ. 2 hits.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 2 hits.
    PROSITEiPS00832. 25A_SYNTH_1. 1 hit.
    PS00833. 25A_SYNTH_2. 1 hit.
    PS50152. 25A_SYNTH_3. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [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 p56 (identifier: Q15646-1) [UniParc]FASTAAdd to Basket

    Also known as: OASL a

    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

    MALMQELYST PASRLDSFVA QWLQPHREWK EEVLDAVRTV EEFLRQEHFQ    50
    GKRGLDQDVR VLKVVKVGSF GNGTVLRSTR EVELVAFLSC FHSFQEAAKH 100
    HKDVLRLIWK TMWQSQDLLD LGLEDLRMEQ RVPDALVFTI QTRGTAEPIT 150
    VTIVPAYRAL GPSLPNSQPP PEVYVSLIKA CGGPGNFCPS FSELQRNFVK 200
    HRPTKLKSLL RLVKHWYQQY VKARSPRANL PPLYALELLT IYAWEMGTEE 250
    DENFMLDEGF TTVMDLLLEY EVICIYWTKY YTLHNAIIED CVRKQLKKER 300
    PIILDPADPT LNVAEGYRWD IVAQRASQCL KQDCCYDNRE NPISSWNVKR 350
    ARDIHLTVEQ RGYPDFNLIV NPYEPIRKVK EKIRRTRGYS GLQRLSFQVP 400
    GSERQLLSSR CSLAKYGIFS HTHIYLLETI PSEIQVFVKN PDGGSYAYAI 450
    NPNSFILGLK QQIEDQQGLP KKQQQLEFQG QVLQDWLGLG IYGIQDSDTL 500
    ILSKKKGEAL FPAS 514
    Length:514
    Mass (Da):59,226
    Last modified:May 30, 2000 - v2
    Checksum:i4D8BB655D9EA003E
    GO
    Isoform p30 (identifier: Q15646-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         220-255: YVKARSPRANLPPLYALELLTIYAWEMGTEEDENFM → AHHPGSGRPHPQRGRRVQMGHRCSEGLPVPETGLLL
         256-514: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:255
    Mass (Da):29,084
    Checksum:iAB54142EF4549492
    GO
    Isoform 3 (identifier: Q15646-3) [UniParc]FASTAAdd to Basket

    Also known as: OASL d

    The sequence of this isoform differs from the canonical sequence as follows:
         220-349: Missing.

    Note: Has antiviral activity against RNA viruses.

    Show »
    Length:384
    Mass (Da):43,942
    Checksum:i7993256048CEFC6D
    GO

    Sequence cautioni

    The sequence AAC41733.1 differs from that shown. Reason: Frameshift at position 386.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 3813HREWK…LDAVR → TGVEGRGARRCA in AAD28541. (PubMed:9826176)CuratedAdd
    BLAST
    Sequence conflicti26 – 3813HREWK…LDAVR → TGVEGRGARRCA in AAD28542. (PubMed:9826176)CuratedAdd
    BLAST
    Sequence conflicti89 – 891S → T in AAD28542. (PubMed:9826176)Curated
    Sequence conflicti95 – 11319QEAAK…WKTMW → PGGSQASQRCSEADMENHV in AAD28541. (PubMed:9826176)CuratedAdd
    BLAST
    Sequence conflicti95 – 11319QEAAK…WKTMW → PGGSQASQRCSEADMENHV in AAD28542. (PubMed:9826176)CuratedAdd
    BLAST
    Sequence conflicti223 – 2231A → S in AAD28541. (PubMed:9826176)Curated
    Sequence conflicti317 – 3171Y → I in AAD28541. (PubMed:9826176)Curated
    Sequence conflicti321 – 3211I → T in AAD28541. (PubMed:9826176)Curated
    Sequence conflicti324 – 3241Q → L in AAD28541. (PubMed:9826176)Curated
    Sequence conflicti341 – 3422NP → KG in AAC41733. (PubMed:7776974)Curated
    Sequence conflicti407 – 4071L → F in BAG37039. (PubMed:14702039)Curated
    Sequence conflicti445 – 4451S → T in AAD28541. (PubMed:9826176)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti341 – 3411N → I.
    Corresponds to variant rs35249920 [ dbSNP | Ensembl ].
    VAR_053544

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei220 – 349130Missing in isoform 3. 1 PublicationVSP_046572Add
    BLAST
    Alternative sequencei220 – 25536YVKAR…DENFM → AHHPGSGRPHPQRGRRVQMG HRCSEGLPVPETGLLL in isoform p30. 1 PublicationVSP_003743Add
    BLAST
    Alternative sequencei256 – 514259Missing in isoform p30. 1 PublicationVSP_003744Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ225089 mRNA. Translation: CAA12396.1.
    AF063611 mRNA. Translation: AAD28541.1.
    AF063612 mRNA. Translation: AAD28542.1.
    JQ792168 mRNA. Translation: AFJ00074.1.
    AK314419 mRNA. Translation: BAG37039.1.
    AC079602 Genomic DNA. No translation available.
    Z93097 Genomic DNA. No translation available.
    BC117408 mRNA. Translation: AAI17409.1.
    BC117410 mRNA. Translation: AAI17411.1.
    L40387 Genomic DNA. Translation: AAC41733.1. Frameshift.
    CCDSiCCDS9211.1. [Q15646-1]
    CCDS9212.1. [Q15646-2]
    RefSeqiNP_001248754.1. NM_001261825.1. [Q15646-3]
    NP_003724.1. NM_003733.3. [Q15646-1]
    NP_937856.1. NM_198213.2. [Q15646-2]
    UniGeneiHs.118633.

    Genome annotation databases

    EnsembliENST00000257570; ENSP00000257570; ENSG00000135114. [Q15646-1]
    ENST00000339275; ENSP00000341125; ENSG00000135114. [Q15646-2]
    GeneIDi8638.
    KEGGihsa:8638.
    UCSCiuc001tzj.2. human. [Q15646-1]
    uc001tzk.2. human. [Q15646-2]

    Polymorphism databases

    DMDMi6226835.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ225089 mRNA. Translation: CAA12396.1 .
    AF063611 mRNA. Translation: AAD28541.1 .
    AF063612 mRNA. Translation: AAD28542.1 .
    JQ792168 mRNA. Translation: AFJ00074.1 .
    AK314419 mRNA. Translation: BAG37039.1 .
    AC079602 Genomic DNA. No translation available.
    Z93097 Genomic DNA. No translation available.
    BC117408 mRNA. Translation: AAI17409.1 .
    BC117410 mRNA. Translation: AAI17411.1 .
    L40387 Genomic DNA. Translation: AAC41733.1 . Frameshift.
    CCDSi CCDS9211.1. [Q15646-1 ]
    CCDS9212.1. [Q15646-2 ]
    RefSeqi NP_001248754.1. NM_001261825.1. [Q15646-3 ]
    NP_003724.1. NM_003733.3. [Q15646-1 ]
    NP_937856.1. NM_198213.2. [Q15646-2 ]
    UniGenei Hs.118633.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WH3 NMR - A 434-507 [» ]
    ProteinModelPortali Q15646.
    SMRi Q15646. Positions 6-346, 368-514.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114191. 3 interactions.
    IntActi Q15646. 1 interaction.
    MINTi MINT-4993190.
    STRINGi 9606.ENSP00000257570.

    PTM databases

    PhosphoSitei Q15646.

    Polymorphism databases

    DMDMi 6226835.

    Proteomic databases

    MaxQBi Q15646.
    PaxDbi Q15646.
    PRIDEi Q15646.

    Protocols and materials databases

    DNASUi 8638.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257570 ; ENSP00000257570 ; ENSG00000135114 . [Q15646-1 ]
    ENST00000339275 ; ENSP00000341125 ; ENSG00000135114 . [Q15646-2 ]
    GeneIDi 8638.
    KEGGi hsa:8638.
    UCSCi uc001tzj.2. human. [Q15646-1 ]
    uc001tzk.2. human. [Q15646-2 ]

    Organism-specific databases

    CTDi 8638.
    GeneCardsi GC12M121459.
    H-InvDB HIX0201831.
    HGNCi HGNC:8090. OASL.
    HPAi HPA001474.
    MIMi 603281. gene.
    neXtProti NX_Q15646.
    PharmGKBi PA31879.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG309765.
    HOGENOMi HOG000022614.
    HOVERGENi HBG000994.
    InParanoidi Q15646.
    KOi K14608.
    OMAi CFHSFQE.
    OrthoDBi EOG7WDN1R.
    PhylomeDBi Q15646.
    TreeFami TF329749.

    Enzyme and pathway databases

    Reactomei REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.

    Miscellaneous databases

    ChiTaRSi OASL. human.
    EvolutionaryTracei Q15646.
    GeneWikii OASL.
    GenomeRNAii 8638.
    NextBioi 32383.
    PROi Q15646.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15646.
    CleanExi HS_OASL.
    Genevestigatori Q15646.

    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.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    PANTHERi PTHR11258. PTHR11258. 1 hit.
    Pfami PF10421. OAS1_C. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    SMARTi SM00213. UBQ. 2 hits.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 2 hits.
    PROSITEi PS00832. 25A_SYNTH_1. 1 hit.
    PS00833. 25A_SYNTH_2. 1 hit.
    PS50152. 25A_SYNTH_3. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "p59OASL, a 2'-5' oligoadenylate synthetase like protein: a novel human gene related to the 2'-5' oligoadenylate synthetase family."
      Hartmann R., Olsen H.S., Widder S., Joergensen R., Justesen J.
      Nucleic Acids Res. 26:4121-4127(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P56).
    2. "Molecular cloning and characterization of two related and interferon-induced 56-kDa and 30-kDa proteins highly similar to 2'-5' oligoadenylate synthetase."
      Rebouillat D., Marie I., Hovanessian A.G.
      Eur. J. Biochem. 257:319-330(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P56 AND P30), FUNCTION, SUBCELLULAR LOCATION.
      Tissue: Monocyte.
    3. "Identification of OASL d, a splice variant of human OASL, with antiviral activity."
      Guo X., Li X., Xu Y., Sun T., Yang G., Wu Z., Li E.
      Int. J. Biochem. Cell Biol. 44:1133-1138(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    4. "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 P56).
      Tissue: Mammary gland.
    5. "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].
    6. "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 P56).
      Tissue: Brain.
    7. "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
      Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
      Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 260-416 (ISOFORM P56).
    8. "Interaction between the 2'-5' oligoadenylate synthetase-like protein p59 OASL and the transcriptional repressor methyl CpG-binding protein 1."
      Andersen J.B., Strandbygaard D.J., Hartmann R., Justesen J.
      Eur. J. Biochem. 271:628-636(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MBD1.
      Tissue: Leukocyte.
    9. "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.
    10. "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.
    11. "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.
    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. "2',5'-Oligoadenylate synthetase-like gene highly induced by hepatitis C virus infection in human liver is inhibitory to viral replication in vitro."
      Ishibashi M., Wakita T., Esumi M.
      Biochem. Biophys. Res. Commun. 392:397-402(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    14. "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.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "Solution structure of C-terminal ubiquitin-like domain of human 2'-5'-oligoadenylate synthetase-like protein (p59 OASL)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 432-507.

    Entry informationi

    Entry nameiOASL_HUMAN
    AccessioniPrimary (citable) accession number: Q15646
    Secondary accession number(s): B2RAZ2
    , I1YDD2, O75686, Q17R95, Q9Y6K6, Q9Y6K7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 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

    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