P00973 (OAS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Catalytic activity	3 ATP = pppA2'p5'A2'p5'A + 2 diphosphate. Ref.20
Cofactor	Magnesium Potential.
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
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
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 process	Antiviral defense Immunity Innate immunity
Cellular component	Cytoplasm Endoplasmic reticulum Microsome Mitochondrion Nucleus Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding RNA-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to interferon-alpha Inferred from direct assay Ref.2. Source: UniProtKB defense response to virus Inferred from direct assay Ref.23. Source: UniProtKB 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-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular_component	cytoplasm 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_function	2'-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.20. 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...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 400

400

2'-5'-oligoadenylate synthase 1

PRO_0000160259

Regions

Region

105 – 158

54

Necessary for binding to dsRNA

Sites

Metal binding

75

1

Magnesium; catalytic Potential

Metal binding

77

1

Magnesium; catalytic Potential

Metal binding

148

1

Magnesium; catalytic Potential

Binding site

210

1

Substrate By similarity

Binding site

213

1

ATP By similarity

Natural variations

Alternative sequence

347 – 400

54

AESNS…TCTIL → TQHTPGSIHPTGRRGLDLHH PLNASASWGKGLQCYLDQFL HFQVGLLIQRGQSSSVSWCI IQDRTQVS in isoform p48.

VSP_003740

Alternative sequence

347 – 382

36

AESNS…HRPST → VNLTLVGRRNYPIISEHAVN LQQTRRASLSYSFQVA in isoform p44.

VSP_027804

Alternative sequence

347 – 364

18

AESNS…RRYQK → VRPPASSLPFIPAPLHEA in isoform p41.

VSP_003738

Alternative sequence

365 – 400

36

Missing in isoform p41.

VSP_003739

Alternative sequence

383 – 400

18

Missing in isoform p44.

VSP_027805

Natural variant

31

1

N → D. Ref.1
Corresponds to variant rs1050994 [ dbSNP | Ensembl ].

VAR_060471

Natural variant

127

1

G → R.
Corresponds to variant rs4767022 [ dbSNP | Ensembl ].

VAR_060472

Natural variant

162

1

G → 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 variant

352

1

A → T. Ref.1 Ref.6 Ref.7
Corresponds to variant rs1131476 [ dbSNP | Ensembl ].

VAR_060473

Natural variant

354

1

D → G.
Corresponds to variant rs35919998 [ dbSNP | Ensembl ].

VAR_057658

Natural variant

361

1

R → T. Ref.1 Ref.6 Ref.7
Corresponds to variant rs1051042 [ dbSNP | Ensembl ].

VAR_057659

Experimental info

Mutagenesis

75

1

D → A: Loss of activity; when associated with A-77. Ref.19

Mutagenesis

77

1

D → A: Loss of activity; when associated with A-75. Ref.19

Mutagenesis

331

1

C → A: Loss of activity; when associated with A-332 and A-333. Ref.18

Mutagenesis

332

1

F → A: Loss of activity; when associated with A-331 and A-333. Ref.18

Mutagenesis

333

1

K → A: Loss of activity; when associated with A-331 and A-332. Ref.18

Sequence conflict

18

1

D → E in AAA39857. Ref.4

Sequence conflict

111

1

R → S in AAH71981. Ref.12

Sequence conflict

115

1

F → L in AAB59552. Ref.1

Sequence conflict

115

1

F → L in AAB59553. Ref.1

Sequence conflict

115

1

F → L in CAA26633. Ref.1

Sequence conflict

120

1

E → V in BAD96726. Ref.10

Sequence conflict

122

1

Q → QE in AAA39858. Ref.4

Sequence conflict

157

1

G → D in AAA39857. Ref.4

Sequence conflict

176

1

E → D in AAA39858. Ref.4

Sequence conflict

295

1

R → T in CAB51602. Ref.2

Sequence conflict

315

1

G → R in CAB51602. Ref.2

Isoform p48:

Sequence conflict

397

1

G → R in AAA39858. Ref.4

Sequence conflict

397

1

G → R in AAW63050. Ref.6

Sequence conflict

397

1

G → R in CAA26497. Ref.16

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

400

Helix Strand Turn

Details...

Turn

4 – 6

3

Helix

9 – 11

3

Helix

12 – 19

8

Helix

24 – 43

20

Turn

44 – 46

3

Beta strand

55 – 61

7

Helix

62 – 66

5

Turn

71 – 73

3

Beta strand

76 – 84

9

Helix

88 – 111

24

Turn

112 – 114

3

Beta strand

116 – 118

3

Beta strand

132 – 137

6

Turn

139 – 141

3

Beta strand

145 – 152

8

Beta strand

161 – 163

3

Helix

167 – 179

13

Turn

183 – 186

4

Helix

187 – 190

4

Helix

191 – 195

5

Turn

196 – 200

5

Helix

203 – 223

21

Helix

229 – 243

15

Helix

251 – 263

13

Helix

265 – 267

3

Beta strand

278 – 280

3

Helix

281 – 290

10

Beta strand

293 – 295

3

Beta strand

297 – 300

4

Beta strand

303 – 308

6

Helix

313 – 326

14

Helix

330 – 332

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform p46 (46 kDa) (E18) [UniParc]. Last modified May 18, 2010. Version 4. Checksum: 03F0A3AA17DAD4E4	FASTA	400	46,029
	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
	Isoform p41 (41 kDa) (E16) (3-9) [UniParc]. Checksum: 2FC9CA8944EC5901	FASTA	364	41,740
	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 SSWILLVRPP ASSLPFIPAP LHEA
	Isoform p48 (9-2) [UniParc]. Checksum: E17B28ECAE185399	FASTA	414	47,408
	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 SSWILLTQHT PGSIHPTGRR 370 380 390 400 410 GLDLHHPLNA SASWGKGLQC YLDQFLHFQV GLLIQRGQSS SVSWCIIQDR TQVS
	Isoform p44 [UniParc]. Checksum: 89654CF4DFFD195C	FASTA	382	43,944
	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 SSWILLVNLT LVGRRNYPII 370 380 SEHAVNLQQT RRASLSYSFQ VA

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00220806.
IPI00305585.
IPI00513823.
IPI00790698.

PIR

SYMSO2. A39417.
SYHU16. A91013.
SYHU18. B24359.
SYMSO3. B39417.

RefSeq

NP_001027581.1. NM_001032409.1.
NP_002525.2. NM_002534.2.
NP_058132.2. NM_016816.2.

UniGene

Hs.524760.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4IG8	X-ray	2.70	A	1-347	[»]

ProteinModelPortal

P00973.

SMR

P00973. Positions 2-346.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00973. 2 interactions.

PTM databases

PhosphoSite

P00973.

Polymorphism databases

DMDM

296439492.

Proteomic databases

PaxDb

P00973.

PRIDE

P00973.

Protocols and materials databases

DNASU

4938.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000202917; ENSP00000202917; ENSG00000089127.
ENST00000445409; ENSP00000388001; ENSG00000089127.
ENST00000452357; ENSP00000415721; ENSG00000089127.

GeneID

4938.

KEGG

hsa:4938.

UCSC

uc001tub.3. human.
uc001tuc.3. human.
uc001tud.3. human.

Organism-specific databases

CTD

4938.

GeneCards

GC12P113344.

HGNC

HGNC:8086. OAS1.

HPA

CAB021104.
HPA003657.

MIM

164350. gene.

neXtProt

NX_P00973.

PharmGKB

PA31875.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG48070.

HOVERGEN

HBG000994.

KO

K14216.

OMA

NWTCTIL.

PhylomeDB

P00973.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000089127-MONOMER.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P00973.

Bgee

P00973.

Genevestigator

P00973.

Family and domain databases

Gene3D

1.10.1410.20. 1 hit.

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.
[Graphical view]

PANTHER

PTHR11258. PTHR11258. 1 hit.

Pfam

PF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 1 hit.
[Graphical view]

PROSITE

PS00832. 25A_SYNTH_1. 1 hit.
PS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

OAS1. human.

GenomeRNAi

4938.

NextBio

19019.

SOURCE

Search...

Entry information

Entry name

OAS1_HUMAN

Accession

Primary (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 history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 146 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.