OAS2
entrez
4939
canonical
uniprot
P29728
canonical
ensembl
ENSG00000111335
resolver
ensp
ENSP00000342278
resolver
ensp
ENSP00000376362
resolver
ensp
ENSP00000411763
resolver
genesymbol
OAS2
resolver
hgnc
HGNC:8087
resolver
uniprot
A8K9T1
resolver
uniprot
Q6PJ33
resolver
uniprot
Q7Z6D0
resolver
uniprot
Q86XX8
resolver
uniprot_entry
OAS2_HUMAN
resolver
uniprot_entry
Q7Z6D0_HUMAN
resolver
uniprot_sec
A8K9T1
resolver
uniprot_sec
Q6PJ33
resolver
uniprot_sec
Q86XX8
resolver
activity_regulation
ACTIVITY REGULATION: Produced as a latent enzyme which is activated by double stranded RNA (dsRNA) generated during the course of viral infection (PubMed:9880569). The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated (PubMed:9880569). ssRNA or dsDNA do not act as activators (PubMed:9880569). Strongly inhibited by copper and iron (PubMed:11682059). Down-regulated by Zn(2+); Zn(2+) stabilizes the homodimeric form that is less responsive than monomers to activation by dsRNA (PubMed:11682059, PubMed:40412389). Partially inhibited by cobalt and nickel ions (PubMed:11682059). {ECO:0000269|PubMed:11682059, ECO:0000269|PubMed:40412389, ECO:0000269|PubMed:9880569}.
uniprot
proteins
amino_acid_sequence
MGNGESQLSSVPAQKLGWFIQEYLKPYEECQTLIDEMVNTICDVLQEPEQFPLVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDQKRSQRDILDKTGDKLKFCLFTKWLKNNFEIQKSLDGFTIQVFTKNQRISFEVLAAFNALSLNDNPSPWIYRELKRSLDKTNASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAWEQGCRKDNFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKICWQWLKKEAQTWLTSPNLDNELPAPSWNVLPAPLFTTPGHLLDKFIKEFLQPNKCFLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKGTALKTGSDADLVVFHNSLKSYTSQKNERHKIVKEIHEQLKAFWREKEEELEVSFEPPKWKAPRVLSFSLKSKVLNESVSFDVLPAFNALGQLSSGSTPSPEVYAGLIDLYKSSDLPGGEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWYKECERKLKPKGSLPPKYALELLTIYAWEQGSGVPDFDTAEGFRTVLELVTQYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAEPTGDVGGGDRWCWHLLAKEAKEWLSSPCFKDGTGNPIPPWKVPTMQTPGSCGARIHPIVNEMFSSRSHRILNNNSKRNF
uniprot
proteins
disease_involvement
DISEASE: Autoinflammation and autoimmunity, systemic, with immune dysregulation 2 (AIAISD2) [MIM:621409]: A disorder characterized by autoimmunity and severe autoinflammation manifesting in the first decade of life, and resulting in hyperinflammatory episodes with cytokine storm. Patients develop vasculitis, rapidly progressive glomerulonephritis, and acute coronary syndrome with myocardial infarction and severe hemorrhagic complications. Death at early age may occur due to cardiocirculatory failure. {ECO:0000269|PubMed:40412389}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.7.84
uniprot
proteins
function
FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:10464285, PubMed:9880569). Activated by detection of double stranded RNA (dsRNA): catalyzes the formation of 2'-5'-oligoadenylates (2-5A) from polymerization of ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation (PubMed:10464285, PubMed:11682059, PubMed:9880569, PubMed:40412389). Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:10464285, PubMed:9880569). Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL (PubMed:21142819). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (PubMed:21142819). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity). {ECO:0000250|UniProtKB:E9Q9A9, ECO:0000269|PubMed:10464285, ECO:0000269|PubMed:11682059, ECO:0000269|PubMed:19923450, ECO:0000269|PubMed:40412389, ECO:0000269|PubMed:9880569, ECO:0000303|PubMed:21142819}.
uniprot
proteins
mass_dalton
82431
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A,D: No loss of activity."; /evidence="ECO:0000269|PubMed:9880569"; MUTAGEN 2; /note="G->A: Loss of localization to Golgi apparatus."; /evidence="ECO:0000269|PubMed:40412389"; MUTAGEN 408; /note="D->A: Loss of activity; when associated with A-410."; /evidence="ECO:0000269|PubMed:10464285"; MUTAGEN 410; /note="D->A: Loss of activity; when associated with A-408."; /evidence="ECO:0000269|PubMed:10464285"; MUTAGEN 421; /note="Y->P,A: Significant loss of activity."; /evidence="ECO:0000269|PubMed:11986302"; MUTAGEN 481; /note="D->A: Loss of activity."; /evidence="ECO:0000269|PubMed:10464285"; MUTAGEN 544; /note="R->A,Y: Significant loss of activity."; /evidence="ECO:0000269|PubMed:11986302"; MUTAGEN 547; /note="K->A: Partial loss of activity."; /evidence="ECO:0000269|PubMed:11986302"; MUTAGEN 652; /note="C->S: Results in dimer-to-monomer transition and increased enzyme activity in the presence of dsRNA."; /evidence="ECO:0000269|PubMed:40412389"; MUTAGEN 668; /note="C->A: Loss of activity; when associated with A-669 and A-670."; /evidence="ECO:0000269|PubMed:10464285"; MUTAGEN 669; /note="F->A: Loss of activity; when associated with A-668 and A-670."; /evidence="ECO:0000269|PubMed:10464285"; MUTAGEN 670; /note="K->A: Loss of activity; when associated with A-668 and A-669."; /evidence="ECO:0000269|PubMed:10464285
uniprot
proteins
post_translational_modification
PTM: Myristoylation is not essential for its activity in vitro. {ECO:0000269|PubMed:2211721, ECO:0000269|PubMed:9880569}.; PTM: Glycosylated. Glycosylation is essential for its activity. {ECO:0000269|PubMed:9880569}.
uniprot
proteins
protein_family
2-5A synthase family
uniprot
proteins
pubmed
10464285
uniprot
proteins
pubmed
11682059
uniprot
proteins
pubmed
11986302
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1577824
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17408844
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19904482
uniprot
proteins
pubmed
19923450
uniprot
proteins
pubmed
21142819
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2211721
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
36538032
uniprot
proteins
pubmed
40412389
uniprot
proteins
pubmed
9880569
uniprot
proteins
sequence_length
719
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19923450}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19923450}. Golgi apparatus membrane {ECO:0000269|PubMed:40412389}.
uniprot
proteins