Reviewed, UniProtKB/Swiss-Prot P00973 (OAS1_HUMAN)

Names and origin

Protein names

Recommended name:
    2'-5'-oligoadenylate synthetase 1
      Short name=(2-5')oligo(A) synthetase 1
      Short name=2-5A synthetase 1
    EC=2.7.7.-
Alternative name(s):
    p46/p42 OAS
    E18/E16

Gene names

Name:	OAS1
Synonyms:	OIAS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a role in mediating resistance to virus infection, control of cell growth, differentiation, and apoptosis.
Catalytic activity	Binds double-stranded RNA and polymerizes ATP into PPP(A2'P5'A)N oligomers, which activate the latent RNase L that, when activated, cleaves single-stranded RNAs.
Subunit structure	Homotetramer.
Subcellular location	Mitochondrion. Nucleus. Microsome. Endoplasmic reticulum. Note: Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions.
Induction	By interferons. Ref.16
Sequence similarities	Belongs to the 2-5A synthetase family.
Caution	Ref.4 sequence was originally thought to originate from mouse.
Sequence caution	The sequence CAA26497.1 differs from that shown. Reason: Frameshift at position 400.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Microsome Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Nucleotidyltransferase Transferase
Gene Ontology (GO)
Biological process	immune response Inferred from electronic annotation. Source: InterPro nucleobase, nucleoside, nucleotide and nucleic acid metabolic process Traceable author statement. Source: ProtInc
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotidyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW
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 synthetase 1		PRO_0000160259
Regions
	Region	105 – 158	54	Necessary for binding to dsRNA
Natural variations
	Alternative sequence	347 – 400	54	AESNS…TCTIL → TQHTPGSIHPTGRRGLDLHH PLNASASWGKGLQCYLDQFL HFQVGLLIQRRQSSSVSWCI 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	162	1	S → G: dbSNP rs1131454. Ref.5 Ref.6 Ref.9		VAR_034872
	Natural variant	354	1	D → G: dbSNP rs35919998.		VAR_057658
	Natural variant	361	1	R → T: dbSNP rs1051042.		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	31	1	N → D in AAB59552. Ref.1
	Sequence conflict	31	1	N → D in AAB59553. Ref.1
	Sequence conflict	31	1	N → D in CAA26633. Ref.1
	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.4
	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
	Sequence conflict	352	1	A → T in AAB59553. Ref.1
	Sequence conflict	352	1	A → T in CAA26634. Ref.1
	Sequence conflict	352	1	A → T in ABE27977. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform p46 (46 kDa) (E18) [UniParc]. Last modified February 21, 2001. Version 3. Checksum: F52BC1717A6C0BC8	FASTA	400	46,059
	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 GSYKPNPQIY 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). Checksum: F1131BC6CB68484E	FASTA	364	41,770
	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 GSYKPNPQIY 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). Checksum: EDE4295CAB5C5399	FASTA	414	47,537
	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 GSYKPNPQIY 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 GLLIQRRQSS SVSWCIIQDR TQVS
	Isoform p44. Checksum: 50B4D1ED0B750488	FASTA	382	43,974
	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 GSYKPNPQIY 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: 2416561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS P41 AND P46), VARIANT 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: 3753689] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P41).
[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: 3754863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P41).
[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: 1651324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS P48 AND P41).
[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), VARIANT GLY-162.
[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: 17024523] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P48), VARIANT 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), VARIANT GLY-162.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P41).
[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).
[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 GLY-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: 16541075] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P41). 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: 3121313] [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: 2830497] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27. 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: 2456211] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27. 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: 2411547] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 231-400 (ISOFORM P41), 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: 6348777] [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: 9407111] [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: 10464285] [Abstract] Cited for: MUTAGENESIS OF ASP-75 AND ASP-77.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X02874 mRNA. Translation: CAA26633.1. X02875 mRNA. Translation: CAA26634.1. M11809 , M11805, M11806, M11807, M11808 Genomic DNA. Translation: AAB59552.1. M11810 Genomic DNA. Translation: AAB59553.1. X04371 mRNA. Translation: CAB51602.1. D00068 mRNA. Translation: BAA00047.1. M63850 Genomic DNA. Translation: AAA39858.1. Different initiation. M63849 Genomic DNA. Translation: AAA39857.1. Different initiation. AY730628 mRNA. Translation: AAW63050.1. AJ629455 mRNA. Translation: CAF33358.1. 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. X07179 Genomic DNA. Translation: CAA30164.1. M18099 Genomic DNA. Translation: AAA59955.1. X02661 mRNA. Translation: CAA26497.1. Frameshift.
IPI	IPI00220806. IPI00305585. IPI00513823. IPI00790698.
PIR	SYMSO2. A39417. SYHU16. A91013. SYHU18. B24359. SYMSO3. B39417.
RefSeq	NP_002525.2.
UniGene	Hs.524760
3D structure databases
SMR	P00973. Positions 2-346.
ModBase	Search...
PTM databases
PhosphoSite	P00973.
Genome annotation databases
Ensembl	ENSG00000089127. Homo sapiens. [Contig view]
GeneID	4938.
Organism-specific databases
GeneCards	GC12P111807.
HGNC	HGNC:8086. OAS1.
HPA	HPA003657.
MIM	164350. gene.
PharmGKB	PA31875.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P00973.
Gene expression databases
ArrayExpress	P00973.
Bgee	P00973.
Family and domain databases
InterPro	IPR006117. 2-5-oligoadenylate_synth_CS. IPR006116. 2-5-oligoadenylate_synth_UB. IPR018952. 2-5-oligoAdlate_synth_1_dom2/C. [Graphical view]
Pfam	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 Resources
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:	February 21, 2001
Last modified:	June 16, 2009
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)