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P00973

- OAS1_HUMAN

UniProt

P00973 - OAS1_HUMAN

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Protein

2'-5'-oligoadenylate synthase 1

Gene

OAS1

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 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.4 Publications

Catalytic activityi

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

Cofactori

Magnesium.1 Publication

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.2 Publications

Kineticsi

  1. KM=0.31 mM for ATP1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631ATP1 Publication
Metal bindingi75 – 751Magnesium; catalytic
Metal bindingi77 – 771Magnesium; catalytic
Metal bindingi148 – 1481Magnesium; catalytic
Sitei158 – 1581Interaction with dsRNA
Binding sitei213 – 2131ATP1 Publication
Binding sitei229 – 2291ATP1 Publication

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. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cellular response to interferon-alpha Source: UniProtKB
  2. cytokine-mediated signaling pathway Source: Reactome
  3. defense response to virus Source: UniProtKB
  4. glucose homeostasis Source: UniProt
  5. glucose metabolic process Source: UniProt
  6. interferon-gamma-mediated signaling pathway Source: Reactome
  7. negative regulation of viral genome replication Source: UniProtKB
  8. protein oligomerization Source: UniProtKB
  9. purine nucleotide biosynthetic process Source: UniProtKB
  10. regulation of ribonuclease activity Source: UniProtKB
  11. response to virus Source: UniProtKB
  12. 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:ENSG00000089127-MONOMER.
ReactomeiREACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
2'-5'-oligoadenylate synthase 1 (EC:2.7.7.84)
Short name:
(2-5')oligo(A) synthase 1
Short name:
2-5A synthase 1
Alternative name(s):
E18/E16
p46/p42 OAS
Gene namesi
Name:OAS1
Synonyms:OIAS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:8086. OAS1.

Subcellular locationi

Cytoplasm 1 Publication. Mitochondrion 1 Publication. Nucleus 1 Publication. Microsome 1 Publication. Endoplasmic reticulum 1 Publication. Secreted By similarity
Note: Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. endoplasmic reticulum Source: UniProtKB-KW
  4. extracellular region Source: UniProtKB-KW
  5. mitochondrion Source: UniProtKB-KW
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661K → A: Decreased enzyme activity. 1 Publication
Mutagenesisi75 – 751D → A: Loss of activity; when associated with A-77. 1 Publication
Mutagenesisi77 – 771D → A: Loss of activity; when associated with A-75. 1 Publication
Mutagenesisi148 – 1481D → A: Strongly reduced enzyme activity. 1 Publication
Mutagenesisi233 – 2331E → A: Loss of enzyme activity. 1 Publication
Mutagenesisi331 – 3311C → A: Loss of activity; when associated with A-332 and A-333. 1 Publication
Mutagenesisi332 – 3321F → A: Loss of activity; when associated with A-331 and A-333. 1 Publication
Mutagenesisi333 – 3331K → A: Loss of activity; when associated with A-331 and A-332. 1 Publication

Organism-specific databases

PharmGKBiPA31875.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4004002'-5'-oligoadenylate synthase 1PRO_0000160259Add
BLAST

Proteomic databases

MaxQBiP00973.
PaxDbiP00973.
PRIDEiP00973.

PTM databases

PhosphoSiteiP00973.

Expressioni

Inductioni

By type I interferon (IFN) and viruses.2 Publications

Gene expression databases

BgeeiP00973.
ExpressionAtlasiP00973. baseline and differential.
GenevestigatoriP00973.

Organism-specific databases

HPAiCAB021104.
HPA003657.

Interactioni

Subunit structurei

Monomer By similarity. Homotetramer.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PRMT6Q96LA82EBI-3932815,EBI-912440

Protein-protein interaction databases

BioGridi110992. 4 interactions.
IntActiP00973. 3 interactions.
MINTiMINT-7003225.

Structurei

Secondary structure

1
400
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63
Helixi9 – 113
Helixi12 – 198
Helixi24 – 4320
Turni44 – 463
Beta strandi55 – 617
Helixi62 – 665
Turni71 – 733
Beta strandi76 – 849
Helixi88 – 11124
Turni112 – 1143
Beta strandi116 – 1183
Beta strandi132 – 1376
Turni139 – 1413
Beta strandi145 – 1528
Beta strandi161 – 1633
Helixi167 – 17913
Turni183 – 1864
Helixi187 – 1904
Helixi191 – 1955
Turni196 – 2005
Helixi203 – 22321
Helixi229 – 24315
Helixi251 – 26313
Helixi265 – 2673
Beta strandi278 – 2803
Helixi281 – 29010
Beta strandi293 – 2953
Beta strandi297 – 3004
Beta strandi303 – 3086
Helixi313 – 32614
Helixi330 – 3323

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IG8X-ray2.70A1-347[»]
ProteinModelPortaliP00973.
SMRiP00973. Positions 3-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 6048Interaction with dsRNAAdd
BLAST
Regioni200 – 21011Interaction with dsRNAAdd
BLAST

Sequence similaritiesi

Belongs to the 2-5A synthase family.Curated

Phylogenomic databases

eggNOGiNOG48070.
GeneTreeiENSGT00510000046406.
HOVERGENiHBG000994.
KOiK14216.
OMAiNCKKKLG.
OrthoDBiEOG7WDN1R.
PhylomeDBiP00973.
TreeFamiTF329749.

Family and domain databases

Gene3Di1.10.1410.20. 1 hit.
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. 1 hit.
[Graphical view]
PROSITEiPS00832. 25A_SYNTH_1. 1 hit.
PS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform p46 (identifier: P00973-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MMDLRNTPAK SLDKFIEDYL LPDTCFRMQI NHAIDIICGF LKERCFRGSS
60 70 80 90 100
YPVCVSKVVK GGSSGKGTTL RGRSDADLVV FLSPLTTFQD QLNRRGEFIQ
110 120 130 140 150
EIRRQLEACQ RERAFSVKFE VQAPRWGNPR ALSFVLSSLQ LGEGVEFDVL
160 170 180 190 200
PAFDALGQLT GGYKPNPQIY VKLIEECTDL QKEGEFSTCF TELQRDFLKQ
210 220 230 240 250
RPTKLKSLIR LVKHWYQNCK KKLGKLPPQY ALELLTVYAW ERGSMKTHFN
260 270 280 290 300
TAQGFRTVLE LVINYQQLCI YWTKYYDFKN PIIEKYLRRQ LTKPRPVILD
310 320 330 340 350
PADPTGNLGG GDPKGWRQLA QEAEAWLNYP CFKNWDGSPV SSWILLAESN
360 370 380 390 400
SADDETDDPR RYQKYGYIGT HEYPHFSHRP STLQAASTPQ AEEDWTCTIL
Length:400
Mass (Da):46,029
Last modified:May 18, 2010 - v4
Checksum:i03F0A3AA17DAD4E4
GO
Isoform p41 (identifier: P00973-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:364
Mass (Da):41,740
Checksum:i2FC9CA8944EC5901
GO
Isoform p48 (identifier: P00973-3) [UniParc]FASTAAdd to Basket

Also known as: 9-2

The sequence of this isoform differs from the canonical sequence as follows:
     347-400: AESNSADDET...AEEDWTCTIL → TQHTPGSIHP...CIIQDRTQVS

Show »
Length:414
Mass (Da):47,408
Checksum:iE17B28ECAE185399
GO
Isoform p44 (identifier: P00973-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:382
Mass (Da):43,944
Checksum:i89654CF4DFFD195C
GO

Sequence cautioni

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 CAA30164.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAA26497.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181D → E in AAA39857. (PubMed:1651324)Curated
Sequence conflicti111 – 1111R → S in AAH71981. (PubMed:15489334)Curated
Sequence conflicti115 – 1151F → L in AAB59552. (PubMed:2416561)Curated
Sequence conflicti115 – 1151F → L in AAB59553. (PubMed:2416561)Curated
Sequence conflicti115 – 1151F → L in CAA26633. (PubMed:2416561)Curated
Sequence conflicti120 – 1201E → V in BAD96726. 1 PublicationCurated
Sequence conflicti122 – 1221Q → QE in AAA39858. (PubMed:1651324)Curated
Sequence conflicti157 – 1571G → D in AAA39857. (PubMed:1651324)Curated
Sequence conflicti176 – 1761E → D in AAA39858. (PubMed:1651324)Curated
Sequence conflicti295 – 2951R → T in CAB51602. (PubMed:3753689)Curated
Sequence conflicti315 – 3151G → R in CAB51602. (PubMed:3753689)Curated
Isoform p48 (identifier: P00973-3)
Sequence conflicti397 – 3971G → R in AAA39858. (PubMed:1651324)Curated
Sequence conflicti397 – 3971G → R in AAW63050. (PubMed:17024523)Curated
Sequence conflicti397 – 3971G → R in CAA26497. (PubMed:2411547)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311N → D.1 Publication
Corresponds to variant rs1050994 [ dbSNP | Ensembl ].
VAR_060471
Natural varianti127 – 1271G → R.
Corresponds to variant rs4767022 [ dbSNP | Ensembl ].
VAR_060472
Natural varianti162 – 1621G → S.9 Publications
Corresponds to variant rs1131454 [ dbSNP | Ensembl ].
VAR_034872
Natural varianti352 – 3521A → T.3 Publications
Corresponds to variant rs1131476 [ dbSNP | Ensembl ].
VAR_060473
Natural varianti354 – 3541D → G.
Corresponds to variant rs35919998 [ dbSNP | Ensembl ].
VAR_057658
Natural varianti361 – 3611R → T.3 Publications
Corresponds to variant rs1051042 [ dbSNP | Ensembl ].
VAR_057659

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei347 – 40054AESNS…TCTIL → TQHTPGSIHPTGRRGLDLHH PLNASASWGKGLQCYLDQFL HFQVGLLIQRGQSSSVSWCI IQDRTQVS in isoform p48. 2 PublicationsVSP_003740Add
BLAST
Alternative sequencei347 – 38236AESNS…HRPST → VNLTLVGRRNYPIISEHAVN LQQTRRASLSYSFQVA in isoform p44. 1 PublicationVSP_027804Add
BLAST
Alternative sequencei347 – 36418AESNS…RRYQK → VRPPASSLPFIPAPLHEA in isoform p41. 8 PublicationsVSP_003738Add
BLAST
Alternative sequencei365 – 40036Missing in isoform p41. 8 PublicationsVSP_003739Add
BLAST
Alternative sequencei383 – 40018Missing in isoform p44. 1 PublicationVSP_027805Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11809
, 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.
CCDSiCCDS31905.1. [P00973-3]
CCDS41838.1. [P00973-1]
CCDS44980.1. [P00973-2]
PIRiA39417. SYMSO2.
A91013. SYHU16.
B24359. SYHU18.
B39417. SYMSO3.
RefSeqiNP_001027581.1. NM_001032409.1. [P00973-3]
NP_002525.2. NM_002534.2. [P00973-2]
NP_058132.2. NM_016816.2. [P00973-1]
UniGeneiHs.524760.

Genome annotation databases

EnsembliENST00000202917; ENSP00000202917; ENSG00000089127. [P00973-1]
ENST00000445409; ENSP00000388001; ENSG00000089127. [P00973-3]
ENST00000452357; ENSP00000415721; ENSG00000089127. [P00973-2]
GeneIDi4938.
KEGGihsa:4938.
UCSCiuc001tub.3. human. [P00973-2]
uc001tuc.3. human. [P00973-3]
uc001tud.3. human. [P00973-1]

Polymorphism databases

DMDMi296439492.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11809
, 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.
CCDSi CCDS31905.1. [P00973-3 ]
CCDS41838.1. [P00973-1 ]
CCDS44980.1. [P00973-2 ]
PIRi A39417. SYMSO2.
A91013. SYHU16.
B24359. SYHU18.
B39417. SYMSO3.
RefSeqi NP_001027581.1. NM_001032409.1. [P00973-3 ]
NP_002525.2. NM_002534.2. [P00973-2 ]
NP_058132.2. NM_016816.2. [P00973-1 ]
UniGenei Hs.524760.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4IG8 X-ray 2.70 A 1-347 [» ]
ProteinModelPortali P00973.
SMRi P00973. Positions 3-346.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110992. 4 interactions.
IntActi P00973. 3 interactions.
MINTi MINT-7003225.

PTM databases

PhosphoSitei P00973.

Polymorphism databases

DMDMi 296439492.

Proteomic databases

MaxQBi P00973.
PaxDbi P00973.
PRIDEi P00973.

Protocols and materials databases

DNASUi 4938.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000202917 ; ENSP00000202917 ; ENSG00000089127 . [P00973-1 ]
ENST00000445409 ; ENSP00000388001 ; ENSG00000089127 . [P00973-3 ]
ENST00000452357 ; ENSP00000415721 ; ENSG00000089127 . [P00973-2 ]
GeneIDi 4938.
KEGGi hsa:4938.
UCSCi uc001tub.3. human. [P00973-2 ]
uc001tuc.3. human. [P00973-3 ]
uc001tud.3. human. [P00973-1 ]

Organism-specific databases

CTDi 4938.
GeneCardsi GC12P113344.
HGNCi HGNC:8086. OAS1.
HPAi CAB021104.
HPA003657.
MIMi 164350. gene.
neXtProti NX_P00973.
PharmGKBi PA31875.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG48070.
GeneTreei ENSGT00510000046406.
HOVERGENi HBG000994.
KOi K14216.
OMAi NCKKKLG.
OrthoDBi EOG7WDN1R.
PhylomeDBi P00973.
TreeFami TF329749.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000089127-MONOMER.
Reactomei REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.

Miscellaneous databases

ChiTaRSi OAS1. human.
GeneWikii OAS1.
GenomeRNAii 4938.
NextBioi 19019.
PROi P00973.
SOURCEi Search...

Gene expression databases

Bgeei P00973.
ExpressionAtlasi P00973. baseline and differential.
Genevestigatori P00973.

Family and domain databases

Gene3Di 1.10.1410.20. 1 hit.
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. 1 hit.
[Graphical view ]
PROSITEi PS00832. 25A_SYNTH_1. 1 hit.
PS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiOAS1_HUMAN
AccessioniPrimary (citable) accession number: P00973
Secondary accession number(s): A8K4N8
, P04820, P29080, P29081, P78485, P78486, Q16700, Q16701, Q1PG42, Q3ZM01, Q53GC5, Q53YA4, Q6A1Z3, Q6IPC6, Q6P7N9, Q96J61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 161 of the entry and version 4 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

Caution

PubMed:1651324 sequence was originally thought to originate from mouse.Curated

Keywords - Technical termi

3D-structure, Complete proteome, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3