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Q9Y6K5

- OAS3_HUMAN

UniProt

Q9Y6K5 - OAS3_HUMAN

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Protein
2'-5'-oligoadenylate synthase 3
Gene
OAS3, P/OKcl.4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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).3 Publications

Catalytic activityi

3 ATP = pppA2'p5'A2'p5'A + 2 diphosphate.

Cofactori

Magnesium Reviewed prediction.

Enzyme regulationi

Produced as a latent enzyme which is activated by dsRNA generated during the course of viral infection. The dsRNA activator must be at least 15 nucleotides long, and no modification of the 2'-hydroxyl group is tolerated. ssRNA or dsDNA do not act as activators.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi816 – 8161Magnesium; catalytic Reviewed prediction
Metal bindingi818 – 8181Magnesium; catalytic Reviewed prediction
Metal bindingi888 – 8881Magnesium; catalytic Reviewed prediction
Binding sitei947 – 9471Substrate By similarity
Binding sitei950 – 9501ATP By similarity

GO - Molecular functioni

  1. 2'-5'-oligoadenylate synthetase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB
  3. double-stranded RNA binding Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. protein binding Source: IntAct

GO - Biological processi

  1. cytokine-mediated signaling pathway Source: Reactome
  2. defense response to virus Source: UniProtKB
  3. interferon-gamma-mediated signaling pathway Source: Reactome
  4. negative regulation of viral genome replication Source: UniProtKB
  5. nucleobase-containing compound metabolic process Source: ProtInc
  6. regulation of ribonuclease activity Source: UniProtKB
  7. response to virus Source: UniProtKB
  8. type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000111331-MONOMER.
ReactomeiREACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
2'-5'-oligoadenylate synthase 3 (EC:2.7.7.84)
Short name:
(2-5')oligo(A) synthase 3
Short name:
2-5A synthase 3
Alternative name(s):
p100 OAS
Short name:
p100OAS
Gene namesi
Name:OAS3
ORF Names:P/OKcl.4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:8088. OAS3.

Subcellular locationi

Cytoplasm. Nucleus 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular space Source: UniProt
  4. intracellular membrane-bounded organelle Source: ProtInc
  5. nucleus Source: HPA
  6. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31877.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 108710872'-5'-oligoadenylate synthase 3
PRO_0000160265Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y6K5.
PaxDbiQ9Y6K5.
PRIDEiQ9Y6K5.

PTM databases

PhosphoSiteiQ9Y6K5.

Expressioni

Tissue specificityi

Present at high level in placenta trophoblast.

Inductioni

By type I interferon (IFN) and viruses.

Gene expression databases

ArrayExpressiQ9Y6K5.
BgeeiQ9Y6K5.
CleanExiHS_OAS3.
GenevestigatoriQ9Y6K5.

Organism-specific databases

HPAiHPA041253.
HPA041372.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
DHX30Q7L2E32EBI-6115729,EBI-1211456
EIF6P565372EBI-6115729,EBI-372243
FTSJ3Q8IY812EBI-6115729,EBI-744088
IFRD2Q128942EBI-6115729,EBI-6115935
MAVSQ7Z4342EBI-6115729,EBI-995373

Protein-protein interaction databases

BioGridi110994. 15 interactions.
IntActiQ9Y6K5. 13 interactions.
MINTiMINT-4991875.
STRINGi9606.ENSP00000228928.

Structurei

3D structure databases

ProteinModelPortaliQ9Y6K5.
SMRiQ9Y6K5. Positions 407-740, 747-1081.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni6 – 343338OAS domain 1
Add
BLAST
Regioni344 – 41067Linker
Add
BLAST
Regioni411 – 742332OAS domain 2
Add
BLAST
Regioni750 – 1084335OAS domain 3
Add
BLAST

Sequence similaritiesi

Belongs to the 2-5A synthase family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG124087.
HOGENOMiHOG000013200.
HOVERGENiHBG007856.
InParanoidiQ9Y6K5.
KOiK14216.
OMAiCQGGEHA.
OrthoDBiEOG7WDN1R.
PhylomeDBiQ9Y6K5.
TreeFamiTF329749.

Family and domain databases

Gene3Di1.10.1410.20. 3 hits.
InterProiIPR006117. 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.
[Graphical view]
PANTHERiPTHR11258. PTHR11258. 1 hit.
PfamiPF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 3 hits.
[Graphical view]
PROSITEiPS00832. 25A_SYNTH_1. 3 hits.
PS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y6K5-1 [UniParc]FASTAAdd to Basket

« Hide

MDLYSTPAAA LDRFVARRLQ PRKEFVEKAR RALGALAAAL RERGGRLGAA     50
APRVLKTVKG GSSGRGTALK GGCDSELVIF LDCFKSYVDQ RARRAEILSE 100
MRASLESWWQ NPVPGLRLTF PEQSVPGALQ FRLTSVDLED WMDVSLVPAF 150
NVLGQAGSGV KPKPQVYSTL LNSGCQGGEH AACFTELRRN FVNIRPAKLK 200
NLILLVKHWY HQVCLQGLWK ETLPPVYALE LLTIFAWEQG CKKDAFSLAE 250
GLRTVLGLIQ QHQHLCVFWT VNYGFEDPAV GQFLQRQLKR PRPVILDPAD 300
PTWDLGNGAA WHWDLLAQEA ASCYDHPCFL RGMGDPVQSW KGPGLPRAGC 350
SGLGHPIQLD PNQKTPENSK SLNAVYPRAG SKPPSCPAPG PTGAASIVPS 400
VPGMALDLSQ IPTKELDRFI QDHLKPSPQF QEQVKKAIDI ILRCLHENCV 450
HKASRVSKGG SFGRGTDLRD GCDVELIIFL NCFTDYKDQG PRRAEILDEM 500
RAQLESWWQD QVPSLSLQFP EQNVPEALQF QLVSTALKSW TDVSLLPAFD 550
AVGQLSSGTK PNPQVYSRLL TSGCQEGEHK ACFAELRRNF MNIRPVKLKN 600
LILLVKHWYR QVAAQNKGKG PAPASLPPAY ALELLTIFAW EQGCRQDCFN 650
MAQGFRTVLG LVQQHQQLCV YWTVNYSTED PAMRMHLLGQ LRKPRPLVLD 700
PADPTWNVGH GSWELLAQEA AALGMQACFL SRDGTSVQPW DVMPALLYQT 750
PAGDLDKFIS EFLQPNRQFL AQVNKAVDTI CSFLKENCFR NSPIKVIKVV 800
KGGSSAKGTA LRGRSDADLV VFLSCFSQFT EQGNKRAEII SEIRAQLEAC 850
QQERQFEVKF EVSKWENPRV LSFSLTSQTM LDQSVDFDVL PAFDALGQLV 900
SGSRPSSQVY VDLIHSYSNA GEYSTCFTEL QRDFIISRPT KLKSLIRLVK 950
HWYQQCTKIS KGRGSLPPQH GLELLTVYAW EQGGKDSQFN MAEGFRTVLE 1000
LVTQYRQLCI YWTINYNAKD KTVGDFLKQQ LQKPRPIILD PADPTGNLGH 1050
NARWDLLAKE AAACTSALCC MGRNGIPIQP WPVKAAV 1087
Length:1,087
Mass (Da):121,170
Last modified:January 11, 2011 - v3
Checksum:i36DAADE4574DE961
GO

Sequence cautioni

The sequence AAD28543.1 differs from that shown. Reason: Frameshift at positions 394 and 398.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181R → K.1 Publication
Corresponds to variant rs1859330 [ dbSNP | Ensembl ].
VAR_060076
Natural varianti18 – 181R → M.
Corresponds to variant rs1859330 [ dbSNP | Ensembl ].
VAR_060077
Natural varianti18 – 181R → T.
Corresponds to variant rs1859330 [ dbSNP | Ensembl ].
VAR_060078
Natural varianti65 – 651R → W.
Corresponds to variant rs12819767 [ dbSNP | Ensembl ].
VAR_057660
Natural varianti378 – 3781R → K.
Corresponds to variant rs45519442 [ dbSNP | Ensembl ].
VAR_062127
Natural varianti381 – 3811S → R.1 Publication
Corresponds to variant rs2285933 [ dbSNP | Ensembl ].
VAR_057661
Natural varianti869 – 8691R → H.
Corresponds to variant rs16942374 [ dbSNP | Ensembl ].
VAR_057662

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591G → A in AAD28543. 1 Publication
Sequence conflicti249 – 2491A → G in AAD28543. 1 Publication
Sequence conflicti287 – 2882QL → HV in AAD28543. 1 Publication
Sequence conflicti316 – 3161L → H in AAD28543. 1 Publication
Sequence conflicti393 – 3931G → A in AAD28543. 1 Publication
Sequence conflicti503 – 5042QL → HV in AAD28543. 1 Publication
Sequence conflicti503 – 5042QL → HV in BAB18647. 1 Publication
Sequence conflicti984 – 9841G → R in BAB18647. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF063613 mRNA. Translation: AAD28543.1. Frameshift.
AB044545 mRNA. Translation: BAB18647.1.
AC004551 Genomic DNA. No translation available.
BC113746 mRNA. Translation: AAI13747.1.
AF251351 Genomic DNA. No translation available.
CCDSiCCDS44981.1.
RefSeqiNP_006178.2. NM_006187.2.
UniGeneiHs.528634.
Hs.744211.

Genome annotation databases

EnsembliENST00000228928; ENSP00000228928; ENSG00000111331.
GeneIDi4940.
KEGGihsa:4940.
UCSCiuc001tug.3. human.

Polymorphism databases

DMDMi317373408.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF063613 mRNA. Translation: AAD28543.1 . Frameshift.
AB044545 mRNA. Translation: BAB18647.1 .
AC004551 Genomic DNA. No translation available.
BC113746 mRNA. Translation: AAI13747.1 .
AF251351 Genomic DNA. No translation available.
CCDSi CCDS44981.1.
RefSeqi NP_006178.2. NM_006187.2.
UniGenei Hs.528634.
Hs.744211.

3D structure databases

ProteinModelPortali Q9Y6K5.
SMRi Q9Y6K5. Positions 407-740, 747-1081.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110994. 15 interactions.
IntActi Q9Y6K5. 13 interactions.
MINTi MINT-4991875.
STRINGi 9606.ENSP00000228928.

PTM databases

PhosphoSitei Q9Y6K5.

Polymorphism databases

DMDMi 317373408.

Proteomic databases

MaxQBi Q9Y6K5.
PaxDbi Q9Y6K5.
PRIDEi Q9Y6K5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000228928 ; ENSP00000228928 ; ENSG00000111331 .
GeneIDi 4940.
KEGGi hsa:4940.
UCSCi uc001tug.3. human.

Organism-specific databases

CTDi 4940.
GeneCardsi GC12P113376.
H-InvDB HIX0201822.
HGNCi HGNC:8088. OAS3.
HPAi HPA041253.
HPA041372.
MIMi 603351. gene.
neXtProti NX_Q9Y6K5.
PharmGKBi PA31877.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG124087.
HOGENOMi HOG000013200.
HOVERGENi HBG007856.
InParanoidi Q9Y6K5.
KOi K14216.
OMAi CQGGEHA.
OrthoDBi EOG7WDN1R.
PhylomeDBi Q9Y6K5.
TreeFami TF329749.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000111331-MONOMER.
Reactomei REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.

Miscellaneous databases

ChiTaRSi OAS3. human.
GeneWikii OAS3.
GenomeRNAii 4940.
NextBioi 19035.
PROi Q9Y6K5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y6K5.
Bgeei Q9Y6K5.
CleanExi HS_OAS3.
Genevestigatori Q9Y6K5.

Family and domain databases

Gene3Di 1.10.1410.20. 3 hits.
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.
IPR002934. Nucleotidyltransferase.
[Graphical view ]
PANTHERi PTHR11258. PTHR11258. 1 hit.
Pfami PF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 3 hits.
[Graphical view ]
PROSITEi PS00832. 25A_SYNTH_1. 3 hits.
PS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The 100-kDa 2',5'-oligoadenylate synthetase catalyzing preferentially the synthesis of dimeric pppA2'p5'A molecules is composed of three homologous domains."
    Rebouillat D., Hovnanian A., Marie I., Hovanessian A.G.
    J. Biol. Chem. 274:1557-1565(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
  2. "Molecular basis of T cell-mediated recognition of pancreatic cancer cells."
    Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N., Itoh K.
    Cancer Res. 61:2038-2046(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-18.
    Tissue: Pancreatic cancer.
  3. "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].
  4. "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], VARIANT ARG-381.
    Tissue: Brain.
  5. "Characterization of the gene encoding the 100-kDa form of human 2', 5'oligoadenylate synthetase."
    Rebouillat D., Hovnanian A., David G., Hovanessian A.G., Williams B.R.
    Genomics 70:232-240(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
    Tissue: Monocyte.
  6. Bienvenut W.V., Gao M., Leug H.
    Submitted (JUN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-17; 118-132; 244-253 AND 371-378, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Prostatic carcinoma.
  7. "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.
  8. "Distinct antiviral roles for human 2',5'-oligoadenylate synthetase family members against dengue virus infection."
    Lin R.J., Yu H.P., Chang B.L., Tang W.C., Liao C.L., Lin Y.L.
    J. Immunol. 183:8035-8043(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "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.
  10. "The large form of human 2',5'-Oligoadenylate Synthetase (OAS3) exerts antiviral effect against Chikungunya virus."
    Brehin A.C., Casademont I., Frenkiel M.P., Julier C., Sakuntabhai A., Despres P.
    Virology 384:216-222(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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.
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiOAS3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6K5
Secondary accession number(s): Q2HJ14, Q9H3P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 118 of the entry and version 3 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

Complete proteome, Direct protein sequencing, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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