ID OAS2_HUMAN Reviewed; 719 AA. AC P29728; A8K9T1; Q6PJ33; Q86XX8; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 196. DE RecName: Full=2'-5'-oligoadenylate synthase 2; DE Short=(2-5')oligo(A) synthase 2; DE Short=2-5A synthase 2; DE EC=2.7.7.84 {ECO:0000269|PubMed:10464285, ECO:0000269|PubMed:11986302, ECO:0000269|PubMed:9880569}; DE AltName: Full=p69 OAS / p71 OAS {ECO:0000303|PubMed:1577824}; DE Short=p69OAS / p71OAS {ECO:0000303|PubMed:1577824}; GN Name=OAS2 {ECO:0000312|HGNC:HGNC:8087}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P69 AND P71), AND INDUCTION. RX PubMed=1577824; DOI=10.1016/s0021-9258(19)50182-x; RA Marie I., Hovanessian A.G.; RT "The 69-kDa 2-5A synthetase is composed of two homologous and adjacent RT functional domains."; RL J. Biol. Chem. 267:9933-9939(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P69). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P69 AND 3). RC TISSUE=Blood, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 420-425 AND 539-547, IDENTIFICATION BY MASS RP SPECTROMETRY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF TYR-421; ARG-544 AND LYS-547. RX PubMed=11986302; DOI=10.1074/jbc.m110202200; RA Sarkar S.N., Miyagi M., Crabb J.W., Sen G.C.; RT "Identification of the substrate-binding sites of 2'-5'-oligoadenylate RT synthetase."; RL J. Biol. Chem. 277:24321-24330(2002). RN [7] RP MYRISTOYLATION AT GLY-2. RX PubMed=2211721; DOI=10.1016/s0021-9258(17)44794-6; RA Marie I., Svab J., Robert N., Galabru J., Hovanessian A.G.; RT "Differential expression and distinct structure of 69- and 100-kDa forms of RT 2-5A synthetase in human cells treated with interferon."; RL J. Biol. Chem. 265:18601-18607(1990). RN [8] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBUNIT, RP ACTIVITY REGULATION, GLYCOSYLATION, MYRISTOYLATION, AND MUTAGENESIS OF RP GLY-2. RX PubMed=9880569; DOI=10.1074/jbc.274.3.1848; RA Sarkar S.N., Bandyopadhyay S., Ghosh A., Sen G.C.; RT "Enzymatic characteristics of recombinant medium isozyme of 2'-5' RT oligoadenylate synthetase."; RL J. Biol. Chem. 274:1848-1855(1999). RN [9] RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF ASP-408; ASP-410; ASP-481; CYS-668; PHE-669 AND LYS-670. RX PubMed=10464285; DOI=10.1074/jbc.274.36.25535; RA Sarkar S.N., Ghosh A., Wang H.W., Sung S.S., Sen G.C.; RT "The nature of the catalytic domain of 2'-5'-oligoadenylate synthetases."; RL J. Biol. Chem. 274:25535-25542(1999). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR. RX PubMed=11682059; DOI=10.1016/s0014-5793(01)02918-0; RA Hartmann R., Walko G., Justesen J.; RT "Inhibition of 2'-5' oligoadenylate synthetase by divalent metal ions."; RL FEBS Lett. 507:54-58(2001). RN [11] RP REVIEW ON FUNCTION. RX PubMed=17408844; DOI=10.1016/j.biochi.2007.02.003; RA Hovanessian A.G., Justesen J.; RT "The human 2'-5'oligoadenylate synthetase family: unique interferon- RT inducible enzymes catalyzing 2'-5' instead of 3'-5' phosphodiester bond RT formation."; RL Biochimie 89:779-788(2007). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19923450; DOI=10.4049/jimmunol.0902728; RA Lin R.J., Yu H.P., Chang B.L., Tang W.C., Liao C.L., Lin Y.L.; RT "Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family RT members against dengue virus infection."; RL J. Immunol. 183:8035-8043(2009). RN [13] RP REVIEW. RX PubMed=19904482; DOI=10.1007/s00239-009-9299-1; RA Kjaer K.H., Poulsen J.B., Reintamm T., Saby E., Martensen P.M., Kelve M., RA Justesen J.; RT "Evolution of the 2'-5'-oligoadenylate synthetase family in eukaryotes and RT bacteria."; RL J. Mol. Evol. 69:612-624(2009). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-378, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP REVIEW ON FUNCTION. RX PubMed=21142819; DOI=10.1089/jir.2010.0107; RA Kristiansen H., Gad H.H., Eskildsen-Larsen S., Despres P., Hartmann R.; RT "The oligoadenylate synthetase family: an ancient protein family with RT multiple antiviral activities."; RL J. Interferon Cytokine Res. 31:41-47(2011). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which CC plays a critical role in cellular innate antiviral response CC (PubMed:10464285, PubMed:9880569). Activated by detection of double CC stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'- CC oligoadenylates (2-5A) from ATP which then bind to the inactive CC monomeric form of ribonuclease L (RNASEL) leading to its dimerization CC and subsequent activation (PubMed:10464285, PubMed:9880569, CC PubMed:11682059). Activation of RNASEL leads to degradation of cellular CC as well as viral RNA, resulting in the inhibition of protein synthesis, CC thus terminating viral replication (PubMed:10464285, PubMed:9880569). CC Can mediate the antiviral effect via the classical RNASEL-dependent CC pathway or an alternative antiviral pathway independent of RNASEL CC (PubMed:21142819). In addition, it may also play a role in other CC cellular processes such as apoptosis, cell growth, differentiation and CC gene regulation (PubMed:21142819). May act as a negative regulator of CC lactation, stopping lactation in virally infected mammary gland CC lobules, thereby preventing transmission of viruses to neonates (By CC similarity). Non-infected lobules would not be affected, allowing CC efficient pup feeding during infection (By similarity). CC {ECO:0000250|UniProtKB:E9Q9A9, ECO:0000269|PubMed:10464285, CC ECO:0000269|PubMed:11682059, ECO:0000269|PubMed:19923450, CC ECO:0000269|PubMed:9880569, ECO:0000303|PubMed:21142819}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')- CC adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84; CC Evidence={ECO:0000269|PubMed:10464285, ECO:0000269|PubMed:11682059, CC ECO:0000269|PubMed:11986302, ECO:0000269|PubMed:9880569}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:11682059}; CC -!- ACTIVITY REGULATION: Produced as a latent enzyme which is activated by CC double stranded RNA (dsRNA) generated during the course of viral CC infection(PubMed:9880569). The dsRNA activator must be at least 15 CC nucleotides long, and no modification of the 2'-hydroxyl group is CC tolerated (PubMed:9880569). ssRNA or dsDNA do not act as activators CC (PubMed:9880569). Strongly inhibited by copper, iron and zinc ions CC (PubMed:11682059). Partially inhibited by cobalt and nickel ions CC (PubMed:11682059). {ECO:0000269|PubMed:11682059, CC ECO:0000269|PubMed:9880569}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.1 mM for ATP {ECO:0000269|PubMed:10464285, CC ECO:0000269|PubMed:11986302, ECO:0000269|PubMed:9880569}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10464285, CC ECO:0000269|PubMed:9880569}. CC -!- INTERACTION: CC P29728; P49761: CLK3; NbExp=4; IntAct=EBI-10211452, EBI-745579; CC P29728-2; P49761: CLK3; NbExp=5; IntAct=EBI-12270678, EBI-745579; CC P29728-2; Q96EF6: FBXO17; NbExp=3; IntAct=EBI-12270678, EBI-2510157; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19923450}. CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:19923450}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=p71 {ECO:0000303|PubMed:1577824}; Synonyms=71 kDa CC {ECO:0000303|PubMed:1577824}; CC IsoId=P29728-1; Sequence=Displayed; CC Name=p69 {ECO:0000303|PubMed:1577824, ECO:0000303|PubMed:2211721}; CC Synonyms=69 kDa {ECO:0000303|PubMed:1577824, CC ECO:0000303|PubMed:2211721}; CC IsoId=P29728-2; Sequence=VSP_003741, VSP_003742; CC Name=3; CC IsoId=P29728-3; Sequence=VSP_043354, VSP_043355; CC -!- INDUCTION: By type I interferon (IFN) and viruses. CC {ECO:0000269|PubMed:1577824}. CC -!- PTM: Myristoylation is not essential for its activity. CC {ECO:0000269|PubMed:2211721, ECO:0000269|PubMed:9880569}. CC -!- PTM: Glycosylated. Glycosylation is essential for its activity. CC {ECO:0000269|PubMed:9880569}. CC -!- SIMILARITY: Belongs to the 2-5A synthase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M87434; AAA60607.1; -; mRNA. DR EMBL; M87284; AAA60606.1; -; mRNA. DR EMBL; AK292796; BAF85485.1; -; mRNA. DR EMBL; AC004551; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW98027.1; -; Genomic_DNA. DR EMBL; BC023637; AAH23637.1; -; mRNA. DR EMBL; BC049215; AAH49215.1; -; mRNA. DR CCDS; CCDS31906.1; -. [P29728-1] DR CCDS; CCDS41839.1; -. [P29728-2] DR CCDS; CCDS44982.1; -. [P29728-3] DR PIR; B42665; B42665. DR RefSeq; NP_001027903.1; NM_001032731.1. [P29728-3] DR RefSeq; NP_002526.2; NM_002535.2. [P29728-2] DR RefSeq; NP_058197.2; NM_016817.2. [P29728-1] DR AlphaFoldDB; P29728; -. DR SMR; P29728; -. DR BioGRID; 110993; 18. DR IntAct; P29728; 5. DR STRING; 9606.ENSP00000342278; -. DR iPTMnet; P29728; -. DR PhosphoSitePlus; P29728; -. DR BioMuta; OAS2; -. DR DMDM; 116242687; -. DR EPD; P29728; -. DR jPOST; P29728; -. DR MassIVE; P29728; -. DR MaxQB; P29728; -. DR PaxDb; 9606-ENSP00000342278; -. DR PeptideAtlas; P29728; -. DR ProteomicsDB; 54606; -. [P29728-1] DR ProteomicsDB; 54607; -. [P29728-2] DR ProteomicsDB; 54608; -. [P29728-3] DR Antibodypedia; 31214; 504 antibodies from 31 providers. DR DNASU; 4939; -. DR Ensembl; ENST00000342315.8; ENSP00000342278.4; ENSG00000111335.14. [P29728-1] DR Ensembl; ENST00000392583.7; ENSP00000376362.3; ENSG00000111335.14. [P29728-2] DR Ensembl; ENST00000449768.2; ENSP00000411763.2; ENSG00000111335.14. [P29728-3] DR GeneID; 4939; -. DR KEGG; hsa:4939; -. DR MANE-Select; ENST00000392583.7; ENSP00000376362.3; NM_002535.3; NP_002526.2. [P29728-2] DR UCSC; uc001tuh.4; human. [P29728-1] DR AGR; HGNC:8087; -. DR CTD; 4939; -. DR DisGeNET; 4939; -. DR GeneCards; OAS2; -. DR HGNC; HGNC:8087; OAS2. DR HPA; ENSG00000111335; Tissue enhanced (salivary). DR MIM; 603350; gene. DR neXtProt; NX_P29728; -. DR OpenTargets; ENSG00000111335; -. DR PharmGKB; PA31876; -. DR VEuPathDB; HostDB:ENSG00000111335; -. DR eggNOG; ENOG502S649; Eukaryota. DR GeneTree; ENSGT00510000046406; -. DR HOGENOM; CLU_026275_0_0_1; -. DR InParanoid; P29728; -. DR OMA; KQCERKM; -. DR OrthoDB; 4638494at2759; -. DR PhylomeDB; P29728; -. DR TreeFam; TF329749; -. DR BioCyc; MetaCyc:ENSG00000111335-MONOMER; -. DR BRENDA; 2.7.7.84; 2681. DR PathwayCommons; P29728; -. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR Reactome; R-HSA-8983711; OAS antiviral response. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR SABIO-RK; P29728; -. DR SignaLink; P29728; -. DR BioGRID-ORCS; 4939; 17 hits in 1164 CRISPR screens. DR ChiTaRS; OAS2; human. DR GeneWiki; OAS2; -. DR GenomeRNAi; 4939; -. DR Pharos; P29728; Tbio. DR PRO; PR:P29728; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P29728; Protein. DR Bgee; ENSG00000111335; Expressed in monocyte and 146 other cell types or tissues. DR ExpressionAtlas; P29728; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IMP:UniProtKB. DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042742; P:defense response to bacterium; IMP:ARUK-UCL. DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB. DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; IDA:ARUK-UCL. DR GO; GO:0045071; P:negative regulation of viral genome replication; IBA:GO_Central. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc. DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:ARUK-UCL. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:ARUK-UCL. DR GO; GO:1903487; P:regulation of lactation; ISS:UniProtKB. DR GO; GO:0009615; P:response to virus; TAS:UniProtKB. DR GO; GO:0006401; P:RNA catabolic process; IEA:Ensembl. DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; ISS:UniProtKB. DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 2. DR Gene3D; 1.10.1410.20; 2'-5'-oligoadenylate synthetase 1, domain 2; 2. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2. DR InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C. DR InterPro; IPR006117; 2-5OAS_C_CS. DR InterPro; IPR043518; 2-5OAS_N_CS. DR InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR PANTHER; PTHR11258:SF3; 2'-5'-OLIGOADENYLATE SYNTHASE 2; 1. DR PANTHER; PTHR11258; 2-5 OLIGOADENYLATE SYNTHETASE; 1. DR Pfam; PF01909; NTP_transf_2; 1. DR Pfam; PF10421; OAS1_C; 2. DR SUPFAM; SSF81301; Nucleotidyltransferase; 2. DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 2. DR PROSITE; PS00832; 25A_SYNTH_1; 2. DR PROSITE; PS00833; 25A_SYNTH_2; 2. DR PROSITE; PS50152; 25A_SYNTH_3; 2. DR Genevisible; P29728; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Antiviral defense; ATP-binding; KW Cytoplasm; Direct protein sequencing; Glycoprotein; Immunity; KW Innate immunity; Lipoprotein; Magnesium; Metal-binding; Myristate; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; Repeat; KW RNA-binding; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2211721" FT CHAIN 2..719 FT /note="2'-5'-oligoadenylate synthase 2" FT /id="PRO_0000160264" FT REGION 11..335 FT /note="OAS domain 1" FT REGION 343..683 FT /note="OAS domain 2" FT BINDING 396 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P00973" FT BINDING 408 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255" FT BINDING 410 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255" FT BINDING 481 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255" FT BINDING 544 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:11986302" FT BINDING 547 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:11986302" FT MOD_RES 378 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:2211721" FT VAR_SEQ 151..172 FT /note="LNDNPSPWIYRELKRSLDKTNA -> KHCWVSGEKSQRSGCQTALCNL (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043354" FT VAR_SEQ 173..719 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043355" FT VAR_SEQ 684..687 FT /note="TMQT -> VKVI (in isoform p69)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1577824" FT /id="VSP_003741" FT VAR_SEQ 688..719 FT /note="Missing (in isoform p69)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1577824" FT /id="VSP_003742" FT MUTAGEN 2 FT /note="G->A,D: No loss of activity." FT /evidence="ECO:0000269|PubMed:9880569" FT MUTAGEN 408 FT /note="D->A: Loss of activity; when associated with A-410." FT /evidence="ECO:0000269|PubMed:10464285" FT MUTAGEN 410 FT /note="D->A: Loss of activity; when associated with A-408." FT /evidence="ECO:0000269|PubMed:10464285" FT MUTAGEN 421 FT /note="Y->P,A: Significant loss of activity." FT /evidence="ECO:0000269|PubMed:11986302" FT MUTAGEN 481 FT /note="D->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:10464285" FT MUTAGEN 544 FT /note="R->A,Y: Significant loss of activity." FT /evidence="ECO:0000269|PubMed:11986302" FT MUTAGEN 547 FT /note="K->A: Partial loss of activity." FT /evidence="ECO:0000269|PubMed:11986302" FT MUTAGEN 668 FT /note="C->A: Loss of activity; when associated with A-669 FT and A-670." FT /evidence="ECO:0000269|PubMed:10464285" FT MUTAGEN 669 FT /note="F->A: Loss of activity; when associated with A-668 FT and A-670." FT /evidence="ECO:0000269|PubMed:10464285" FT MUTAGEN 670 FT /note="K->A: Loss of activity; when associated with A-668 FT and A-669." FT /evidence="ECO:0000269|PubMed:10464285" FT CONFLICT 45..47 FT /note="LQE -> CRN (in Ref. 1; AAA60607/AAA60606)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="F -> S (in Ref. 1; AAA60607/AAA60606)" FT /evidence="ECO:0000305" FT CONFLICT 606 FT /note="C -> G (in Ref. 1; AAA60607/AAA60606)" FT /evidence="ECO:0000305" FT CONFLICT 639 FT /note="A -> G (in Ref. 1; AAA60607/AAA60606)" FT /evidence="ECO:0000305" FT CONFLICT 657 FT /note="A -> D (in Ref. 1; AAA60607/AAA60606)" FT /evidence="ECO:0000305" FT CONFLICT 662..663 FT /note="EW -> VR (in Ref. 1; AAA60607/AAA60606)" FT /evidence="ECO:0000305" FT CONFLICT 719 FT /note="F -> FWRSSGNRF (in Ref. 1; AAA60607)" FT /evidence="ECO:0000305" SQ SEQUENCE 719 AA; 82431 MW; 1B680D397D5EDB78 CRC64; MGNGESQLSS VPAQKLGWFI QEYLKPYEEC QTLIDEMVNT ICDVLQEPEQ FPLVQGVAIG GSYGRKTVLR GNSDGTLVLF FSDLKQFQDQ KRSQRDILDK TGDKLKFCLF TKWLKNNFEI QKSLDGFTIQ VFTKNQRISF EVLAAFNALS LNDNPSPWIY RELKRSLDKT NASPGEFAVC FTELQQKFFD NRPGKLKDLI LLIKHWHQQC QKKIKDLPSL SPYALELLTV YAWEQGCRKD NFDIAEGVRT VLELIKCQEK LCIYWMVNYN FEDETIRNIL LHQLQSARPV ILDPVDPTNN VSGDKICWQW LKKEAQTWLT SPNLDNELPA PSWNVLPAPL FTTPGHLLDK FIKEFLQPNK CFLEQIDSAV NIIRTFLKEN CFRQSTAKIQ IVRGGSTAKG TALKTGSDAD LVVFHNSLKS YTSQKNERHK IVKEIHEQLK AFWREKEEEL EVSFEPPKWK APRVLSFSLK SKVLNESVSF DVLPAFNALG QLSSGSTPSP EVYAGLIDLY KSSDLPGGEF STCFTVLQRN FIRSRPTKLK DLIRLVKHWY KECERKLKPK GSLPPKYALE LLTIYAWEQG SGVPDFDTAE GFRTVLELVT QYQQLCIFWK VNYNFEDETV RKFLLSQLQK TRPVILDPAE PTGDVGGGDR WCWHLLAKEA KEWLSSPCFK DGTGNPIPPW KVPTMQTPGS CGARIHPIVN EMFSSRSHRI LNNNSKRNF //