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P00973 (OAS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2'-5'-oligoadenylate synthase 1

Short name=(2-5')oligo(A) synthase 1
Short name=2-5A synthase 1
EC=2.7.7.84
Alternative name(s):
E18/E16
p46/p42 OAS
Gene names
Name:OAS1
Synonyms:OIAS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L. Ref.20 Ref.22 Ref.23 Ref.28

Catalytic activity

3 ATP = pppA2'p5'A2'p5'A + 2 diphosphate. Ref.20 Ref.28

Cofactor

Magnesium. Ref.28

Enzyme regulation

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. Ref.20 Ref.28

Subunit structure

Monomer By similarity. Homotetramer.

Subcellular location

Cytoplasm. Mitochondrion. Nucleus. Microsome. Endoplasmic reticulum. Secreted By similarity. Note: Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions. Ref.23

Induction

By type I interferon (IFN) and viruses. Ref.16 Ref.20 Ref.24 Ref.28

Sequence similarities

Belongs to the 2-5A synthase family.

Caution

Ref.4 sequence was originally thought to originate from mouse.

Biophysicochemical properties

Kinetic parameters:

KM=0.31 mM for ATP Ref.20

Sequence caution

The sequence AAA39857.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAA39858.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAA59955.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAD96726.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA26497.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAA30164.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
   Cellular componentCytoplasm
Endoplasmic reticulum
Microsome
Mitochondrion
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionNucleotidyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to interferon-alpha

Inferred from direct assay Ref.2. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response to virus

Inferred from direct assay Ref.23. Source: UniProtKB

glucose homeostasis

Inferred from mutant phenotype PubMed 23575436. Source: UniProt

glucose metabolic process

Inferred from mutant phenotype PubMed 23575436. Source: UniProt

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

negative regulation of viral genome replication

Inferred from direct assay Ref.22Ref.23. Source: UniProtKB

protein oligomerization

Inferred from direct assay PubMed 11682059. Source: UniProtKB

purine nucleotide biosynthetic process

Inferred from direct assay PubMed 11682059Ref.2Ref.3. Source: UniProtKB

regulation of ribonuclease activity

Inferred from direct assay Ref.23. Source: UniProtKB

response to virus

Inferred from direct assay Ref.22. Source: UniProtKB

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.23Ref.2Ref.3. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_function2'-5'-oligoadenylate synthetase activity

Inferred from direct assay Ref.20PubMed 11682059Ref.2Ref.3. Source: UniProtKB

ATP binding

Traceable author statement Ref.27. Source: UniProtKB

double-stranded RNA binding

Inferred from direct assay Ref.20Ref.28. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from direct assay PubMed 11682059. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRMT6Q96LA82EBI-3932815,EBI-912440

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform p46 (identifier: P00973-1)

Also known as: 46 kDa; E18;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform p41 (identifier: P00973-2)

Also known as: 41 kDa; E16; 3-9;

The sequence of this isoform differs from the canonical sequence as follows:
     347-364: AESNSADDETDDPRRYQK → VRPPASSLPFIPAPLHEA
     365-400: Missing.
Isoform p48 (identifier: P00973-3)

Also known as: 9-2;

The sequence of this isoform differs from the canonical sequence as follows:
     347-400: AESNSADDET...AEEDWTCTIL → TQHTPGSIHP...CIIQDRTQVS
Isoform p44 (identifier: P00973-4)

The sequence of this isoform differs from the canonical sequence as follows:
     347-382: AESNSADDETDDPRRYQKYGYIGTHEYPHFSHRPST → VNLTLVGRRNYPIISEHAVNLQQTRRASLSYSFQVA
     383-400: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4004002'-5'-oligoadenylate synthase 1
PRO_0000160259

Regions

Region13 – 6048Interaction with dsRNA
Region200 – 21011Interaction with dsRNA

Sites

Metal binding751Magnesium; catalytic
Metal binding771Magnesium; catalytic
Metal binding1481Magnesium; catalytic
Binding site631ATP
Binding site2131ATP
Binding site2291ATP
Site1581Interaction with dsRNA

Natural variations

Alternative sequence347 – 40054AESNS…TCTIL → TQHTPGSIHPTGRRGLDLHH PLNASASWGKGLQCYLDQFL HFQVGLLIQRGQSSSVSWCI IQDRTQVS in isoform p48.
VSP_003740
Alternative sequence347 – 38236AESNS…HRPST → VNLTLVGRRNYPIISEHAVN LQQTRRASLSYSFQVA in isoform p44.
VSP_027804
Alternative sequence347 – 36418AESNS…RRYQK → VRPPASSLPFIPAPLHEA in isoform p41.
VSP_003738
Alternative sequence365 – 40036Missing in isoform p41.
VSP_003739
Alternative sequence383 – 40018Missing in isoform p44.
VSP_027805
Natural variant311N → D. Ref.1
Corresponds to variant rs1050994 [ dbSNP | Ensembl ].
VAR_060471
Natural variant1271G → R.
Corresponds to variant rs4767022 [ dbSNP | Ensembl ].
VAR_060472
Natural variant1621G → S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.8 Ref.9 Ref.10 Ref.12
Corresponds to variant rs1131454 [ dbSNP | Ensembl ].
VAR_034872
Natural variant3521A → T. Ref.1 Ref.6 Ref.7
Corresponds to variant rs1131476 [ dbSNP | Ensembl ].
VAR_060473
Natural variant3541D → G.
Corresponds to variant rs35919998 [ dbSNP | Ensembl ].
VAR_057658
Natural variant3611R → T. Ref.1 Ref.6 Ref.7
Corresponds to variant rs1051042 [ dbSNP | Ensembl ].
VAR_057659

Experimental info

Mutagenesis661K → A: Decreased enzyme activity. Ref.28
Mutagenesis751D → A: Loss of activity; when associated with A-77. Ref.19
Mutagenesis771D → A: Loss of activity; when associated with A-75. Ref.19
Mutagenesis1481D → A: Strongly reduced enzyme activity. Ref.28
Mutagenesis2331E → A: Loss of enzyme activity. Ref.28
Mutagenesis3311C → A: Loss of activity; when associated with A-332 and A-333. Ref.18
Mutagenesis3321F → A: Loss of activity; when associated with A-331 and A-333. Ref.18
Mutagenesis3331K → A: Loss of activity; when associated with A-331 and A-332. Ref.18
Sequence conflict181D → E in AAA39857. Ref.4
Sequence conflict1111R → S in AAH71981. Ref.12
Sequence conflict1151F → L in AAB59552. Ref.1
Sequence conflict1151F → L in AAB59553. Ref.1
Sequence conflict1151F → L in CAA26633. Ref.1
Sequence conflict1201E → V in BAD96726. Ref.10
Sequence conflict1221Q → QE in AAA39858. Ref.4
Sequence conflict1571G → D in AAA39857. Ref.4
Sequence conflict1761E → D in AAA39858. Ref.4
Sequence conflict2951R → T in CAB51602. Ref.2
Sequence conflict3151G → R in CAB51602. Ref.2
Isoform p48:
Sequence conflict3971G → R in AAA39858. Ref.4
Sequence conflict3971G → R in AAW63050. Ref.6
Sequence conflict3971G → R in CAA26497. Ref.16

Secondary structure

......................................................... 400
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform p46 (46 kDa) (E18) [UniParc].

Last modified May 18, 2010. Version 4.
Checksum: 03F0A3AA17DAD4E4

FASTA40046,029
        10         20         30         40         50         60 
MMDLRNTPAK SLDKFIEDYL LPDTCFRMQI NHAIDIICGF LKERCFRGSS YPVCVSKVVK 

        70         80         90        100        110        120 
GGSSGKGTTL RGRSDADLVV FLSPLTTFQD QLNRRGEFIQ EIRRQLEACQ RERAFSVKFE 

       130        140        150        160        170        180 
VQAPRWGNPR ALSFVLSSLQ LGEGVEFDVL PAFDALGQLT GGYKPNPQIY VKLIEECTDL 

       190        200        210        220        230        240 
QKEGEFSTCF TELQRDFLKQ RPTKLKSLIR LVKHWYQNCK KKLGKLPPQY ALELLTVYAW 

       250        260        270        280        290        300 
ERGSMKTHFN TAQGFRTVLE LVINYQQLCI YWTKYYDFKN PIIEKYLRRQ LTKPRPVILD 

       310        320        330        340        350        360 
PADPTGNLGG GDPKGWRQLA QEAEAWLNYP CFKNWDGSPV SSWILLAESN SADDETDDPR 

       370        380        390        400 
RYQKYGYIGT HEYPHFSHRP STLQAASTPQ AEEDWTCTIL 

« Hide

Isoform p41 (41 kDa) (E16) (3-9) [UniParc].

Checksum: 2FC9CA8944EC5901
Show »

FASTA36441,740
Isoform p48 (9-2) [UniParc].

Checksum: E17B28ECAE185399
Show »

FASTA41447,408
Isoform p44 [UniParc].

Checksum: 89654CF4DFFD195C
Show »

FASTA38243,944

References

« Hide 'large scale' references
[1]"Structure of two forms of the interferon-induced (2'-5') oligo A synthetase of human cells based on cDNAs and gene sequences."
Benech P., Mory Y., Revel M., Chebath J.
EMBO J. 4:2249-2256(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS P41 AND P46), VARIANTS ASP-31; SER-162; THR-352 AND THR-361.
Tissue: Fetal blood.
[2]"Full-length sequence and expression of the 42 kDa 2-5A synthetase induced by human interferon."
Wathelet M.G., Moutschen S., Cravador A., Dewit L., Defilippi P., Huez G.A., Content J.
FEBS Lett. 196:113-120(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P41), VARIANT SER-162.
[3]"Structure and expression of a cloned cDNA for human (2'-5')oligoadenylate synthetase."
Shiojiri S., Fukunaga R., Ichii Y., Sokawa Y.
J. Biochem. 99:1455-1464(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P41), VARIANT SER-162.
[4]"Cloning, sequencing, and expression of two murine 2'-5'-oligoadenylate synthetases. Structure-function relationships."
Ghosh S.K., Kusari J., Bandyopadhyay S.K., Samanta H., Kumar R., Sen G.C.
J. Biol. Chem. 266:15293-15299(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS P48 AND P41), VARIANT SER-162.
[5]"OAS1p44, a splice variant of the interferon induced human 2'-5' oligoadenylate synthetase."
Andersen J.B., Strandbygaard D.J., Larsen S.E., Justesen J.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P44).
[6]"The mammalian 2'-5' oligoadenylate synthetase gene family: evidence for concerted evolution of paralogous Oas1 genes in Rodentia and Artiodactyla."
Perelygin A.A., Zharkikh A.A., Scherbik S.V., Brinton M.A.
J. Mol. Evol. 63:562-576(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P48), VARIANTS SER-162; THR-352 AND THR-361.
[7]"Susceptibility to infection by West Nile Virus: OAS1 (OAS1 2'-5' oligoadenylate synthetase gene) stop codon detected in exon 1 of a normal individual heterozygous for the gene."
Lee M.-K., Morshed M.G., Jorgensen D.R., Hasselback P., Goh S.-H.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM P46), VARIANTS THR-352 AND THR-361.
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P41), VARIANT SER-162.
[9]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P41), VARIANT SER-162.
[10]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P41), VARIANT SER-162.
Tissue: Small intestine.
[11]"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. expand/collapse author list , 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].
[12]"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] (ISOFORM P41), VARIANT SER-162.
Tissue: Brain and Uterus.
[13]"New inducers revealed by the promoter sequence analysis of two interferon-activated human genes."
Wathelet M.G., Clauss I.M., Nols C.B., Content J., Huez G.A.
Eur. J. Biochem. 169:313-321(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[14]"Interferon-responsive regulatory elements in the promoter of the human 2',5'-oligo(A) synthetase gene."
Benech P., Vigneron M., Peretz D., Revel M., Chebath J.
Mol. Cell. Biol. 7:4498-4504(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
Tissue: Liver.
[15]"Interferon-induced binding of nuclear factors to promoter elements of the 2-5A synthetase gene."
Rutherford M.N., Hannigan G.E., Williams B.R.G.
EMBO J. 7:751-759(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
Tissue: Liver.
[16]"Human 2-5A synthetase: characterization of a novel cDNA and corresponding gene structure."
Saunders M.E., Gewert D.R., Tugwell M.E., McMahon M., Williams B.R.G.
EMBO J. 4:1761-1768(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 231-400 (ISOFORM P48), INDUCTION.
Tissue: Lymphoblast.
[17]"Molecular cloning and sequence of partial cDNA for interferon-induced (2'-5')oligo(A) synthetase mRNA from human cells."
Merlin G., Chebath J., Benech P., Metz R., Revel M.
Proc. Natl. Acad. Sci. U.S.A. 80:4904-4908(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 255-364 (ISOFORM P41).
[18]"Enzymatic activity of 2'-5'-oligoadenylate synthetase is impaired by specific mutations that affect oligomerization of the protein."
Ghosh A., Sarkar S.N., Guo W., Bandyopadhyay S., Sen G.C.
J. Biol. Chem. 272:33220-33226(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-331; PHE-332 AND LYS-333.
[19]"The nature of the catalytic domain of 2'-5'-oligoadenylate synthetases."
Sarkar S.N., Ghosh A., Wang H.W., Sung S.S., Sen G.C.
J. Biol. Chem. 274:25535-25542(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-75 AND ASP-77.
[20]"Characterization of the 2'-5'-oligoadenylate synthetase ubiquitin-like family."
Eskildsen S., Justesen J., Schierup M.H., Hartmann R.
Nucleic Acids Res. 31:3166-3173(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[21]"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.
[22]"The p59 oligoadenylate synthetase-like protein possesses antiviral activity that requires the C-terminal ubiquitin-like domain."
Marques J., Anwar J., Eskildsen-Larsen S., Rebouillat D., Paludan S.R., Sen G., Williams B.R., Hartmann R.
J. Gen. Virol. 89:2767-2772(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]"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.
[24]"Differential regulation of the OASL and OAS1 genes in response to viral infections."
Melchjorsen J., Kristiansen H., Christiansen R., Rintahaka J., Matikainen S., Paludan S.R., Hartmann R.
J. Interferon Cytokine Res. 29:199-207(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[25]"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.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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.
[28]"Structural basis for cytosolic double-stranded RNA surveillance by human oligoadenylate synthetase 1."
Donovan J., Dufner M., Korennykh A.
Proc. Natl. Acad. Sci. U.S.A. 110:1652-1657(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-347 IN COMPLEX WITH DSRNA; MAGNESIUM IONS AND ATP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF LYS-66; ASP-148 AND GLU-233.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11809 expand/collapse EMBL AC list , M11805, M11806, M11807, M11808 Genomic DNA. Translation: AAB59552.1.
M11810 Genomic DNA. Translation: AAB59553.1.
X02874 mRNA. Translation: CAA26633.1.
X02875 mRNA. Translation: CAA26634.1.
X04371 mRNA. Translation: CAB51602.1.
D00068 mRNA. Translation: BAA00047.1.
M63849 Genomic DNA. Translation: AAA39857.1. Different initiation.
M63850 Genomic DNA. Translation: AAA39858.1. Different initiation.
AJ629455 mRNA. Translation: CAF33358.1.
AY730628 mRNA. Translation: AAW63050.1.
DQ445949 Genomic DNA. Translation: ABE27977.1.
AK291003 mRNA. Translation: BAF83692.1.
BT006785 mRNA. Translation: AAP35431.1.
AK223006 mRNA. Translation: BAD96726.1. Different initiation.
AC004551 Genomic DNA. No translation available.
BC000562 mRNA. Translation: AAH00562.4.
BC061587 mRNA. Translation: AAH61587.1.
BC071981 mRNA. Translation: AAH71981.3.
X06560 Genomic DNA. Translation: CAA29803.1.
M18099 Genomic DNA. Translation: AAA59955.1. Different initiation.
X07179 Genomic DNA. Translation: CAA30164.1. Different initiation.
X02661 mRNA. Translation: CAA26497.1. Sequence problems.
PIRSYMSO2. A39417.
SYHU16. A91013.
SYHU18. B24359.
SYMSO3. B39417.
RefSeqNP_001027581.1. NM_001032409.1.
NP_002525.2. NM_002534.2.
NP_058132.2. NM_016816.2.
UniGeneHs.524760.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IG8X-ray2.70A1-347[»]
ProteinModelPortalP00973.
SMRP00973. Positions 3-346.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110992. 4 interactions.
IntActP00973. 3 interactions.
MINTMINT-7003225.

PTM databases

PhosphoSiteP00973.

Polymorphism databases

DMDM296439492.

Proteomic databases

PaxDbP00973.
PRIDEP00973.

Protocols and materials databases

DNASU4938.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000202917; ENSP00000202917; ENSG00000089127. [P00973-1]
ENST00000445409; ENSP00000388001; ENSG00000089127. [P00973-3]
ENST00000452357; ENSP00000415721; ENSG00000089127. [P00973-2]
GeneID4938.
KEGGhsa:4938.
UCSCuc001tub.3. human. [P00973-2]
uc001tuc.3. human. [P00973-3]
uc001tud.3. human. [P00973-1]

Organism-specific databases

CTD4938.
GeneCardsGC12P113344.
HGNCHGNC:8086. OAS1.
HPACAB021104.
HPA003657.
MIM164350. gene.
neXtProtNX_P00973.
PharmGKBPA31875.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG48070.
HOVERGENHBG000994.
KOK14216.
OMANCKKKLG.
OrthoDBEOG7WDN1R.
PhylomeDBP00973.
TreeFamTF329749.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000089127-MONOMER.
ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP00973.
BgeeP00973.
GenevestigatorP00973.

Family and domain databases

Gene3D1.10.1410.20. 1 hit.
InterProIPR006117. 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]
PANTHERPTHR11258. PTHR11258. 1 hit.
PfamPF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 1 hit.
[Graphical view]
PROSITEPS00832. 25A_SYNTH_1. 1 hit.
PS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSOAS1. human.
GeneWikiOAS1.
GenomeRNAi4938.
NextBio19019.
PROP00973.
SOURCESearch...

Entry information

Entry nameOAS1_HUMAN
AccessionPrimary (citable) accession number: P00973
Secondary accession number(s): A8K4N8 expand/collapse secondary AC list , P04820, P29080, P29081, P78485, P78486, Q16700, Q16701, Q1PG42, Q3ZM01, Q53GC5, Q53YA4, Q6A1Z3, Q6IPC6, Q6P7N9, Q96J61
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 155 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM