P29728 (OAS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2'-5'-oligoadenylate synthase 2
Short name=(2-5')oligo(A) synthase 2
Short name=2-5A synthase 2
EC=2.7.7.-

Alternative name(s):
p69 OAS / p71 OAS
Short name=p69OAS / p71OAS

Gene names

Name:

OAS2

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	719 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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	Homodimer.
Subcellular location	Mitochondrion. Nucleus. Microsome. Endoplasmic reticulum. Note: Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions. Ref.6
Induction	By interferons.
Sequence similarities	Belongs to the 2-5A synthase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Microsome Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Nucleotidyltransferase Transferase
PTM	Acetylation Lipoprotein Myristate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome nucleobase-containing compound metabolic process Traceable author statement. Source: ProtInc purine nucleotide biosynthetic process Inferred from direct assay. Source: UniProtKB type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB cytosol Traceable author statement. Source: Reactome endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Traceable author statement. Source: ProtInc microsome Traceable author statement. Source: ProtInc 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. Source: UniProtKB 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 zinc ion binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform p71 (identifier: P29728-1)

Also known as: 71 kDa;

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 p69 (identifier: P29728-2)

Also known as: 69 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     684-687: TMQT → VKVI
     688-719: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Probable
	Chain	2 – 719	718	2'-5'-oligoadenylate synthase 2		PRO_0000160264
Regions
	Region	11 – 335	325	OAS domain 1
	Region	343 – 683	341	OAS domain 2
	Compositional bias	326 – 346	21	Pro-rich (linker)
Amino acid modifications
	Modified residue	378	1	N6-acetyllysine Ref.8
	Modified residue	433	1	N6-acetyllysine Ref.8
	Lipidation	2	1	N-myristoyl glycine Ref.6
Natural variations
	Alternative sequence	684 – 687	4	TMQT → VKVI in isoform p69.		VSP_003741
	Alternative sequence	688 – 719	32	Missing in isoform p69.		VSP_003742
Experimental info
	Mutagenesis	408	1	D → A: Loss of activity; when associated with A-410. Ref.7
	Mutagenesis	410	1	D → A: Loss of activity; when associated with A-408. Ref.7
	Mutagenesis	481	1	D → A: Loss of activity. Ref.7
	Mutagenesis	668	1	C → A: Loss of activity; when associated with A-669 and A-670. Ref.7
	Mutagenesis	669	1	F → A: Loss of activity; when associated with A-668 and A-670. Ref.7
	Mutagenesis	670	1	K → A: Loss of activity; when associated with A-668 and A-669. Ref.7
	Sequence conflict	45 – 47	3	LQE → CRN in AAA60607. Ref.1
	Sequence conflict	45 – 47	3	LQE → CRN in AAA60606. Ref.1
	Sequence conflict	127	1	F → S in AAA60607. Ref.1
	Sequence conflict	127	1	F → S in AAA60606. Ref.1
	Sequence conflict	606	1	C → G in AAA60607. Ref.1
	Sequence conflict	606	1	C → G in AAA60606. Ref.1
	Sequence conflict	639	1	A → G in AAA60607. Ref.1
	Sequence conflict	639	1	A → G in AAA60606. Ref.1
	Sequence conflict	657	1	A → D in AAA60607. Ref.1
	Sequence conflict	657	1	A → D in AAA60606. Ref.1
	Sequence conflict	662 – 663	2	EW → VR in AAA60607. Ref.1
	Sequence conflict	662 – 663	2	EW → VR in AAA60606. Ref.1
	Sequence conflict	719	1	F → FWRSSGNRF in AAA60607. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform p71 (71 kDa) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1B680D397D5EDB78	FASTA	719	82,431
	10 20 30 40 50 60 MGNGESQLSS VPAQKLGWFI QEYLKPYEEC QTLIDEMVNT ICDVLQEPEQ FPLVQGVAIG 70 80 90 100 110 120 GSYGRKTVLR GNSDGTLVLF FSDLKQFQDQ KRSQRDILDK TGDKLKFCLF TKWLKNNFEI 130 140 150 160 170 180 QKSLDGFTIQ VFTKNQRISF EVLAAFNALS LNDNPSPWIY RELKRSLDKT NASPGEFAVC 190 200 210 220 230 240 FTELQQKFFD NRPGKLKDLI LLIKHWHQQC QKKIKDLPSL SPYALELLTV YAWEQGCRKD 250 260 270 280 290 300 NFDIAEGVRT VLELIKCQEK LCIYWMVNYN FEDETIRNIL LHQLQSARPV ILDPVDPTNN 310 320 330 340 350 360 VSGDKICWQW LKKEAQTWLT SPNLDNELPA PSWNVLPAPL FTTPGHLLDK FIKEFLQPNK 370 380 390 400 410 420 CFLEQIDSAV NIIRTFLKEN CFRQSTAKIQ IVRGGSTAKG TALKTGSDAD LVVFHNSLKS 430 440 450 460 470 480 YTSQKNERHK IVKEIHEQLK AFWREKEEEL EVSFEPPKWK APRVLSFSLK SKVLNESVSF 490 500 510 520 530 540 DVLPAFNALG QLSSGSTPSP EVYAGLIDLY KSSDLPGGEF STCFTVLQRN FIRSRPTKLK 550 560 570 580 590 600 DLIRLVKHWY KECERKLKPK GSLPPKYALE LLTIYAWEQG SGVPDFDTAE GFRTVLELVT 610 620 630 640 650 660 QYQQLCIFWK VNYNFEDETV RKFLLSQLQK TRPVILDPAE PTGDVGGGDR WCWHLLAKEA 670 680 690 700 710 KEWLSSPCFK DGTGNPIPPW KVPTMQTPGS CGARIHPIVN EMFSSRSHRI LNNNSKRNF
	Isoform p69 (69 kDa) [UniParc]. Checksum: 34729B5A88A38B2D	FASTA	687	78,787
	10 20 30 40 50 60 MGNGESQLSS VPAQKLGWFI QEYLKPYEEC QTLIDEMVNT ICDVLQEPEQ FPLVQGVAIG 70 80 90 100 110 120 GSYGRKTVLR GNSDGTLVLF FSDLKQFQDQ KRSQRDILDK TGDKLKFCLF TKWLKNNFEI 130 140 150 160 170 180 QKSLDGFTIQ VFTKNQRISF EVLAAFNALS LNDNPSPWIY RELKRSLDKT NASPGEFAVC 190 200 210 220 230 240 FTELQQKFFD NRPGKLKDLI LLIKHWHQQC QKKIKDLPSL SPYALELLTV YAWEQGCRKD 250 260 270 280 290 300 NFDIAEGVRT VLELIKCQEK LCIYWMVNYN FEDETIRNIL LHQLQSARPV ILDPVDPTNN 310 320 330 340 350 360 VSGDKICWQW LKKEAQTWLT SPNLDNELPA PSWNVLPAPL FTTPGHLLDK FIKEFLQPNK 370 380 390 400 410 420 CFLEQIDSAV NIIRTFLKEN CFRQSTAKIQ IVRGGSTAKG TALKTGSDAD LVVFHNSLKS 430 440 450 460 470 480 YTSQKNERHK IVKEIHEQLK AFWREKEEEL EVSFEPPKWK APRVLSFSLK SKVLNESVSF 490 500 510 520 530 540 DVLPAFNALG QLSSGSTPSP EVYAGLIDLY KSSDLPGGEF STCFTVLQRN FIRSRPTKLK 550 560 570 580 590 600 DLIRLVKHWY KECERKLKPK GSLPPKYALE LLTIYAWEQG SGVPDFDTAE GFRTVLELVT 610 620 630 640 650 660 QYQQLCIFWK VNYNFEDETV RKFLLSQLQK TRPVILDPAE PTGDVGGGDR WCWHLLAKEA 670 680 KEWLSSPCFK DGTGNPIPPW KVPVKVI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The 69-kDa 2-5A synthetase is composed of two homologous and adjacent functional domains." Marie I., Hovanessian A.G. J. Biol. Chem. 267:9933-9939(1992) [PubMed: 1577824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P69 AND P71).
[2]	"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 P69). Tissue: Trachea.
[3]	"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].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 P69). Tissue: Uterus.
[6]	"Differential expression and distinct structure of 69- and 100-kDa forms of 2-5A synthetase in human cells treated with interferon." Marie I., Svab J., Robert N., Galabru J., Hovanessian A.G. J. Biol. Chem. 265:18601-18607(1990) [PubMed: 2211721] [Abstract] Cited for: MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION.
[7]	"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-408; ASP-410; ASP-481; CYS-668; PHE-669 AND LYS-670.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-378 AND LYS-433, MASS SPECTROMETRY.
[9]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M87434 mRNA. Translation: AAA60607.1. M87284 mRNA. Translation: AAA60606.1. AK292796 mRNA. Translation: BAF85485.1. AC004551 Genomic DNA. No translation available. CH471054 Genomic DNA. Translation: EAW98027.1. BC049215 mRNA. Translation: AAH49215.1.
IPI	IPI00217049. IPI00218185.
PIR	B42665.
RefSeq	NP_002526.2. NM_002535.2. NP_058197.2. NM_016817.2.
UniGene	Hs.414332.
3D structure databases
ProteinModelPortal	P29728.
SMR	P29728. Positions 6-336, 338-684.
ModBase	Search...
Protein-protein interaction databases
STRING	P29728.
PTM databases
PhosphoSite	P29728.
Polymorphism databases
DMDM	116242687.
Proteomic databases
PRIDE	P29728.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000342315; ENSP00000342278; ENSG00000111335.
GeneID	4939.
KEGG	hsa:4939.
UCSC	uc001tui.1. human. uc001tuj.1. human.
Organism-specific databases
CTD	4939.
GeneCards	GC12P113416.
HGNC	HGNC:8087. OAS2.
HPA	CAB024984.
MIM	603350. gene.
neXtProt	NX_P29728.
PharmGKB	PA31876.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16199.
GeneTree	ENSGT00510000046406.
HOGENOM	HBG126488.
HOVERGEN	HBG007855.
InParanoid	P29728.
OMA	GGDRWCW.
OrthoDB	EOG4GTKD5.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P29728.
Bgee	P29728.
CleanEx	HS_OAS2.
Genevestigator	P29728.
GermOnline	ENSG00000111335. Homo sapiens.
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. 2 hits.
KO	K14216.
Pfam	PF01909. NTP_transf_2. 1 hit. PF10421. OAS1_C. 2 hits. [Graphical view]
PROSITE	PS00832. 25A_SYNTH_1. 2 hits. PS00833. 25A_SYNTH_2. 2 hits. PS50152. 25A_SYNTH_3. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	19027.
SOURCE	Search...

Entry information

Entry name

OAS2_HUMAN

Accession

Primary (citable) accession number: P29728
Secondary accession number(s): A8K9T1, Q86XX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 107 of the entry and version 3 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.