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.-

Alternative name(s):
E18/E16
p46/p42 OAS

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.
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 synthase family.
Caution	Ref.4 sequence was originally thought to originate from mouse.
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
Cellular component	Endoplasmic reticulum Microsome Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	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. Source: UniProtKB interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome negative regulation of viral genome replication Inferred from direct assay. Source: UniProtKB protein oligomerization Inferred from direct assay. Source: UniProtKB purine nucleotide biosynthetic process Inferred from direct assay Ref.2Ref.3. Source: UniProtKB regulation of ribonuclease activity Inferred from direct assay. Source: UniProtKB type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular component	cytoplasm Inferred from direct assay Ref.2Ref.3. Source: UniProtKB cytosol Traceable author statement. Source: Reactome 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
Molecular function	2'-5'-oligoadenylate synthetase activity Inferred from direct assay Ref.2Ref.3. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW double-stranded RNA binding Inferred from sequence or structural similarity. Source: UniProtKB nucleotidyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from direct assay. 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
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	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
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
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

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: 2416561] [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: 3753689] [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: 3754863] [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: 1651324] [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: 17024523] [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: 14702039] [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: 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), 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: 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 1-28. 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: 2456211] [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: 2411547] [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: 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
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
ProteinModelPortal	P00973.
SMR	P00973. Positions 2-346.
ModBase	Search...
Protein-protein interaction databases
IntAct	P00973. 2 interactions.
STRING	P00973.
PTM databases
PhosphoSite	P00973.
Polymorphism databases
DMDM	296439492.
Proteomic databases
PRIDE	P00973.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000202917; ENSP00000202917; ENSG00000089127.
GeneID	4938.
KEGG	hsa:4938.
UCSC	uc001tub.1. human. uc001tud.1. 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
HOVERGEN	HBG000994.
PhylomeDB	P00973.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P00973.
Bgee	P00973.
Genevestigator	P00973.
Family and domain databases
InterPro	IPR006117. 2-5-oligoadenylate_synth_CS. IPR006116. 2-5-oligoadenylate_synth_N. IPR018952. 2-5-oligoAdlate_synth_1_dom2/C. IPR002934. Nucleotidyltransferase. [Graphical view]
Gene3D	G3DSA:1.10.1410.20. 2-5-oligoAdlate_synth_1_dom2/C. 1 hit.
KO	K14216.
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
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:	January 25, 2012
This is version 133 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.