CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024012
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2'-5'-oligoadenylate synthase 3 
Protein Synonyms/Alias
 (2-5')oligo(A) synthase 3; 2-5A synthase 3; p100 OAS; p100OAS 
Gene Name
 OAS3 
Gene Synonyms/Alias
 P/OKcl.4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
341GDPVQSWKGPGLPRAubiquitination[1]
458HKASRVSKGGSFGRGubiquitination[2, 3]
580GCQEGEHKACFAELRubiquitination[2]
807VKGGSSAKGTALRGRubiquitination[2]
1059ARWDLLAKEAAACTSubiquitination[2]
1084PIQPWPVKAAV****ubiquitination[2]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 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). 
Sequence Annotation
 REGION 6 343 OAS domain 1.
 REGION 344 410 Linker.
 REGION 411 742 OAS domain 2.
 REGION 750 1084 OAS domain 3.
 METAL 816 816 Magnesium; catalytic (Potential).
 METAL 818 818 Magnesium; catalytic (Potential).
 METAL 888 888 Magnesium; catalytic (Potential).
 BINDING 947 947 Substrate (By similarity).
 BINDING 950 950 ATP (By similarity).
 MOD_RES 1 1 N-acetylmethionine.  
Keyword
 Acetylation; Antiviral defense; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Immunity; Innate immunity; Magnesium; Metal-binding; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome; Repeat; RNA-binding; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1087 AA 
Protein Sequence
MDLYSTPAAA LDRFVARRLQ PRKEFVEKAR RALGALAAAL RERGGRLGAA APRVLKTVKG 60
GSSGRGTALK GGCDSELVIF LDCFKSYVDQ RARRAEILSE MRASLESWWQ NPVPGLRLTF 120
PEQSVPGALQ FRLTSVDLED WMDVSLVPAF NVLGQAGSGV KPKPQVYSTL LNSGCQGGEH 180
AACFTELRRN FVNIRPAKLK NLILLVKHWY HQVCLQGLWK ETLPPVYALE LLTIFAWEQG 240
CKKDAFSLAE GLRTVLGLIQ QHQHLCVFWT VNYGFEDPAV GQFLQRQLKR PRPVILDPAD 300
PTWDLGNGAA WHWDLLAQEA ASCYDHPCFL RGMGDPVQSW KGPGLPRAGC SGLGHPIQLD 360
PNQKTPENSK SLNAVYPRAG SKPPSCPAPG PTGAASIVPS VPGMALDLSQ IPTKELDRFI 420
QDHLKPSPQF QEQVKKAIDI ILRCLHENCV HKASRVSKGG SFGRGTDLRD GCDVELIIFL 480
NCFTDYKDQG PRRAEILDEM RAQLESWWQD QVPSLSLQFP EQNVPEALQF QLVSTALKSW 540
TDVSLLPAFD AVGQLSSGTK PNPQVYSRLL TSGCQEGEHK ACFAELRRNF MNIRPVKLKN 600
LILLVKHWYR QVAAQNKGKG PAPASLPPAY ALELLTIFAW EQGCRQDCFN MAQGFRTVLG 660
LVQQHQQLCV YWTVNYSTED PAMRMHLLGQ LRKPRPLVLD PADPTWNVGH GSWELLAQEA 720
AALGMQACFL SRDGTSVQPW DVMPALLYQT PAGDLDKFIS EFLQPNRQFL AQVNKAVDTI 780
CSFLKENCFR NSPIKVIKVV KGGSSAKGTA LRGRSDADLV VFLSCFSQFT EQGNKRAEII 840
SEIRAQLEAC QQERQFEVKF EVSKWENPRV LSFSLTSQTM LDQSVDFDVL PAFDALGQLV 900
SGSRPSSQVY VDLIHSYSNA GEYSTCFTEL QRDFIISRPT KLKSLIRLVK HWYQQCTKIS 960
KGRGSLPPQH GLELLTVYAW EQGGKDSQFN MAEGFRTVLE LVTQYRQLCI YWTINYNAKD 1020
KTVGDFLKQQ LQKPRPIILD PADPTGNLGH NARWDLLAKE AAACTSALCC MGRNGIPIQP 1080
WPVKAAV 1087 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0051607; P:defense response to virus; IDA:UniProtKB.
 GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
 GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
 GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
 GO:0060700; P:regulation of ribonuclease activity; IDA:UniProtKB.
 GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome. 
Interpro
 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. 
Pfam
 PF01909; NTP_transf_2
 PF10421; OAS1_C 
SMART
  
PROSITE
 PS00832; 25A_SYNTH_1
 PS00833; 25A_SYNTH_2
 PS50152; 25A_SYNTH_3 
PRINTS