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P29728 (OAS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2'-5'-oligoadenylate synthase 2

Short name=(2-5')oligo(A) synthase 2
Short name=2-5A synthase 2
EC=2.7.7.84
Alternative name(s):
p69 OAS / p71 OAS
Short name=p69OAS / p71OAS
Gene names
Name:OAS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length719 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.8 Ref.9 Ref.11

Catalytic activity

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

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.8

Subunit structure

Homodimer. Ref.8 Ref.9

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. Mitochondrion. Nucleus. Microsome. Endoplasmic reticulum. Note: Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions. Ref.7 Ref.11

Induction

By type I interferon (IFN) and viruses. Ref.8

Post-translational modification

Myristoylation is not essential for its activity.

Glycosylated. Glycosylation is essential for its activity. Ref.8

Sequence similarities

Belongs to the 2-5A synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=2.1 mM for ATP Ref.6 Ref.8 Ref.9

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
   Cellular componentCytoplasm
Endoplasmic reticulum
Microsome
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
RNA-binding
   Molecular functionNucleotidyltransferase
Transferase
   PTMAcetylation
Glycoprotein
Lipoprotein
Myristate
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA catabolic process

Inferred from electronic annotation. Source: Ensembl

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

nucleobase-containing compound metabolic process

Traceable author statement PubMed 2440675. Source: ProtInc

protein glycosylation

Inferred from direct assay Ref.8. Source: UniProtKB

protein myristoylation

Inferred from mutant phenotype Ref.8. Source: UniProtKB

purine nucleotide biosynthetic process

Inferred from direct assay PubMed 11682059. Source: UniProtKB

response to virus

Traceable author statement Ref.15. Source: UniProtKB

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular membrane-bounded organelle

Traceable author statement PubMed 2440675. Source: ProtInc

membrane

Traceable author statement PubMed 2440675. Source: ProtInc

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_function2'-5'-oligoadenylate synthetase activity

Inferred from direct assay Ref.8PubMed 11682059. Source: UniProtKB

ATP binding

Inferred from mutant phenotype Ref.9. Source: UniProtKB

double-stranded RNA binding

Inferred from direct assay Ref.8. 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 3 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.
Isoform 3 (identifier: P29728-3)

The sequence of this isoform differs from the canonical sequence as follows:
     151-172: LNDNPSPWIYRELKRSLDKTNA → KHCWVSGEKSQRSGCQTALCNL
     173-719: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 7197182'-5'-oligoadenylate synthase 2
PRO_0000160264

Regions

Region11 – 335325OAS domain 1
Region343 – 683341OAS domain 2
Compositional bias326 – 34621Pro-rich (linker)

Sites

Metal binding4081Magnesium; catalytic Potential
Metal binding4101Magnesium; catalytic Potential
Metal binding4811Magnesium; catalytic Potential
Binding site5441Substrate
Binding site5471ATP

Amino acid modifications

Modified residue3781N6-acetyllysine Ref.13
Lipidation21N-myristoyl glycine Ref.7 Ref.8

Natural variations

Alternative sequence151 – 17222LNDNP…DKTNA → KHCWVSGEKSQRSGCQTALC NL in isoform 3.
VSP_043354
Alternative sequence173 – 719547Missing in isoform 3.
VSP_043355
Alternative sequence684 – 6874TMQT → VKVI in isoform p69.
VSP_003741
Alternative sequence688 – 71932Missing in isoform p69.
VSP_003742

Experimental info

Mutagenesis21G → A or D: No loss of activity. Ref.8
Mutagenesis4081D → A: Loss of activity; when associated with A-410. Ref.9
Mutagenesis4101D → A: Loss of activity; when associated with A-408. Ref.9
Mutagenesis4211Y → P or A: Significant loss of activity. Ref.6
Mutagenesis4811D → A: Loss of activity. Ref.9
Mutagenesis5441R → A or Y: Significant loss of activity. Ref.6
Mutagenesis5471K → A: Partial loss of activity. Ref.6
Mutagenesis6681C → A: Loss of activity; when associated with A-669 and A-670. Ref.9
Mutagenesis6691F → A: Loss of activity; when associated with A-668 and A-670. Ref.9
Mutagenesis6701K → A: Loss of activity; when associated with A-668 and A-669. Ref.9
Sequence conflict45 – 473LQE → CRN in AAA60607. Ref.1
Sequence conflict45 – 473LQE → CRN in AAA60606. Ref.1
Sequence conflict1271F → S in AAA60607. Ref.1
Sequence conflict1271F → S in AAA60606. Ref.1
Sequence conflict6061C → G in AAA60607. Ref.1
Sequence conflict6061C → G in AAA60606. Ref.1
Sequence conflict6391A → G in AAA60607. Ref.1
Sequence conflict6391A → G in AAA60606. Ref.1
Sequence conflict6571A → D in AAA60607. Ref.1
Sequence conflict6571A → D in AAA60606. Ref.1
Sequence conflict662 – 6632EW → VR in AAA60607. Ref.1
Sequence conflict662 – 6632EW → VR in AAA60606. Ref.1
Sequence conflict7191F → FWRSSGNRF in AAA60607. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform p71 (71 kDa) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1B680D397D5EDB78

FASTA71982,431
        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 

« Hide

Isoform p69 (69 kDa) [UniParc].

Checksum: 34729B5A88A38B2D
Show »

FASTA68778,787
Isoform 3 [UniParc].

Checksum: 8CF5C0C9EE9850A9
Show »

FASTA17219,517

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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 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. expand/collapse author list , 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].
[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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P69 AND 3).
Tissue: Blood and Uterus.
[6]"Identification of the substrate-binding sites of 2'-5'-oligoadenylate synthetase."
Sarkar S.N., Miyagi M., Crabb J.W., Sen G.C.
J. Biol. Chem. 277:24321-24330(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 420-425 AND 539-547, IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-421; ARG-544 AND LYS-547.
[7]"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] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION.
[8]"Enzymatic characteristics of recombinant medium isozyme of 2'-5' oligoadenylate synthetase."
Sarkar S.N., Bandyopadhyay S., Ghosh A., Sen G.C.
J. Biol. Chem. 274:1848-1855(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION, GLYCOSYLATION, MYRISTOYLATION, MUTAGENESIS OF GLY-2.
[9]"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: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-408; ASP-410; ASP-481; CYS-668; PHE-669 AND LYS-670.
[10]"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.
[11]"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.
[12]"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.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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].
[15]"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
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.
BC023637 mRNA. Translation: AAH23637.1.
BC049215 mRNA. Translation: AAH49215.1.
PIRB42665.
RefSeqNP_001027903.1. NM_001032731.1.
NP_002526.2. NM_002535.2.
NP_058197.2. NM_016817.2.
UniGeneHs.414332.

3D structure databases

ProteinModelPortalP29728.
SMRP29728. Positions 7-336, 340-680.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110993. 2 interactions.
STRING9606.ENSP00000342278.

PTM databases

PhosphoSiteP29728.

Polymorphism databases

DMDM116242687.

Proteomic databases

PaxDbP29728.
PRIDEP29728.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342315; ENSP00000342278; ENSG00000111335. [P29728-1]
ENST00000392583; ENSP00000376362; ENSG00000111335. [P29728-2]
ENST00000449768; ENSP00000411763; ENSG00000111335. [P29728-3]
GeneID4939.
KEGGhsa:4939.
UCSCuc001tuh.3. human. [P29728-3]
uc001tui.1. human. [P29728-2]
uc001tuj.3. human. [P29728-1]

Organism-specific databases

CTD4939.
GeneCardsGC12P113416.
H-InvDBHIX0129679.
HGNCHGNC:8087. OAS2.
HPACAB024984.
MIM603350. gene.
neXtProtNX_P29728.
PharmGKBPA31876.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG124087.
HOGENOMHOG000013200.
HOVERGENHBG007855.
InParanoidP29728.
KOK14216.
OMAKSYTSQK.
OrthoDBEOG7WDN1R.
PhylomeDBP29728.
TreeFamTF329749.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000111335-MONOMER.
ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP29728.
BgeeP29728.
CleanExHS_OAS2.
GenevestigatorP29728.

Family and domain databases

Gene3D1.10.1410.20. 2 hits.
InterProIPR006117. 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]
PANTHERPTHR11258. PTHR11258. 1 hit.
PfamPF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 2 hits.
[Graphical view]
PROSITEPS00832. 25A_SYNTH_1. 2 hits.
PS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

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Entry information

Entry nameOAS2_HUMAN
AccessionPrimary (citable) accession number: P29728
Secondary accession number(s): A8K9T1, Q6PJ33, Q86XX8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM