CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005808
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2'-5'-oligoadenylate synthase 2 
Protein Synonyms/Alias
 (2-5')oligo(A) synthase 2; 2-5A synthase 2; p69 OAS / p71 OAS; p69OAS / p71OAS 
Gene Name
 OAS2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
112LKFCLFTKWLKNNFEubiquitination[1]
360KEFLQPNKCFLEQIDubiquitination[2]
378NIIRTFLKENCFRQSacetylation[3]
419VVFHNSLKSYTSQKNubiquitination[1]
433NERHKIVKEIHEQLKacetylation[3]
470RVLSFSLKSKVLNESubiquitination[1]
472LSFSLKSKVLNESVSubiquitination[1]
Reference
 [1] 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]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
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 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. 
Sequence Annotation
 REGION 11 335 OAS domain 1.
 REGION 343 683 OAS domain 2.
 METAL 408 408 Magnesium; catalytic (Potential).
 METAL 410 410 Magnesium; catalytic (Potential).
 METAL 481 481 Magnesium; catalytic (Potential).
 BINDING 544 544 Substrate.
 BINDING 547 547 ATP.
 MOD_RES 378 378 N6-acetyllysine.
 LIPID 2 2 N-myristoyl glycine.  
Keyword
 Acetylation; Alternative splicing; Antiviral defense; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Immunity; Innate immunity; Lipoprotein; Magnesium; Metal-binding; Microsome; Mitochondrion; Myristate; Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; RNA-binding; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 719 AA 
Protein Sequence
MGNGESQLSS VPAQKLGWFI QEYLKPYEEC QTLIDEMVNT ICDVLQEPEQ FPLVQGVAIG 60
GSYGRKTVLR GNSDGTLVLF FSDLKQFQDQ KRSQRDILDK TGDKLKFCLF TKWLKNNFEI 120
QKSLDGFTIQ VFTKNQRISF EVLAAFNALS LNDNPSPWIY RELKRSLDKT NASPGEFAVC 180
FTELQQKFFD NRPGKLKDLI LLIKHWHQQC QKKIKDLPSL SPYALELLTV YAWEQGCRKD 240
NFDIAEGVRT VLELIKCQEK LCIYWMVNYN FEDETIRNIL LHQLQSARPV ILDPVDPTNN 300
VSGDKICWQW LKKEAQTWLT SPNLDNELPA PSWNVLPAPL FTTPGHLLDK FIKEFLQPNK 360
CFLEQIDSAV NIIRTFLKEN CFRQSTAKIQ IVRGGSTAKG TALKTGSDAD LVVFHNSLKS 420
YTSQKNERHK IVKEIHEQLK AFWREKEEEL EVSFEPPKWK APRVLSFSLK SKVLNESVSF 480
DVLPAFNALG QLSSGSTPSP EVYAGLIDLY KSSDLPGGEF STCFTVLQRN FIRSRPTKLK 540
DLIRLVKHWY KECERKLKPK GSLPPKYALE LLTIYAWEQG SGVPDFDTAE GFRTVLELVT 600
QYQQLCIFWK VNYNFEDETV RKFLLSQLQK TRPVILDPAE PTGDVGGGDR WCWHLLAKEA 660
KEWLSSPCFK DGTGNPIPPW KVPTMQTPGS CGARIHPIVN EMFSSRSHRI LNNNSKRNF 719 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc.
 GO:0016020; C:membrane; TAS:ProtInc.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IMP:UniProtKB.
 GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
 GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
 GO:0006486; P:protein glycosylation; IDA:UniProtKB.
 GO:0018377; P:protein myristoylation; IMP:UniProtKB.
 GO:0006164; P:purine nucleotide biosynthetic process; IDA:UniProtKB.
 GO:0009615; P:response to virus; TAS:UniProtKB.
 GO:0006401; P:RNA catabolic process; IEA:Compara.
 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