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P29728

- OAS2_HUMAN

UniProt

P29728 - OAS2_HUMAN

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Protein

2'-5'-oligoadenylate synthase 2

Gene

OAS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

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

Cofactori

Magnesium.Curated

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=2.1 mM for ATP3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi408 – 4081Magnesium; catalyticSequence Analysis
Metal bindingi410 – 4101Magnesium; catalyticSequence Analysis
Metal bindingi481 – 4811Magnesium; catalyticSequence Analysis
Binding sitei544 – 5441Substrate
Binding sitei547 – 5471ATP

GO - Molecular functioni

  1. 2'-5'-oligoadenylate synthetase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB
  3. double-stranded RNA binding Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cytokine-mediated signaling pathway Source: Reactome
  2. defense response to virus Source: UniProtKB-KW
  3. interferon-gamma-mediated signaling pathway Source: Reactome
  4. nucleobase-containing compound metabolic process Source: ProtInc
  5. protein glycosylation Source: UniProtKB
  6. protein myristoylation Source: UniProtKB
  7. purine nucleotide biosynthetic process Source: UniProtKB
  8. response to virus Source: UniProtKB
  9. RNA catabolic process Source: Ensembl
  10. type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000111335-MONOMER.
ReactomeiREACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
2'-5'-oligoadenylate synthase 2 (EC:2.7.7.84)
Short name:
(2-5')oligo(A) synthase 2
Short name:
2-5A synthase 2
Alternative name(s):
p69 OAS / p71 OAS
Short name:
p69OAS / p71OAS
Gene namesi
Name:OAS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:8087. OAS2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. endoplasmic reticulum Source: UniProtKB-KW
  4. intracellular membrane-bounded organelle Source: ProtInc
  5. membrane Source: UniProtKB
  6. mitochondrion Source: UniProtKB-KW
  7. nucleus Source: UniProtKB-KW
  8. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A or D: No loss of activity. 1 Publication
Mutagenesisi408 – 4081D → A: Loss of activity; when associated with A-410. 1 Publication
Mutagenesisi410 – 4101D → A: Loss of activity; when associated with A-408. 1 Publication
Mutagenesisi421 – 4211Y → P or A: Significant loss of activity. 1 Publication
Mutagenesisi481 – 4811D → A: Loss of activity. 1 Publication
Mutagenesisi544 – 5441R → A or Y: Significant loss of activity. 1 Publication
Mutagenesisi547 – 5471K → A: Partial loss of activity. 1 Publication
Mutagenesisi668 – 6681C → A: Loss of activity; when associated with A-669 and A-670. 1 Publication
Mutagenesisi669 – 6691F → A: Loss of activity; when associated with A-668 and A-670. 1 Publication
Mutagenesisi670 – 6701K → A: Loss of activity; when associated with A-668 and A-669. 1 Publication

Organism-specific databases

PharmGKBiPA31876.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 7197182'-5'-oligoadenylate synthase 2PRO_0000160264Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei378 – 3781N6-acetyllysine1 Publication

Post-translational modificationi

Myristoylation is not essential for its activity.2 Publications
Glycosylated. Glycosylation is essential for its activity.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Lipoprotein, Myristate

Proteomic databases

MaxQBiP29728.
PaxDbiP29728.
PRIDEiP29728.

PTM databases

PhosphoSiteiP29728.

Expressioni

Inductioni

By type I interferon (IFN) and viruses.

Gene expression databases

BgeeiP29728.
CleanExiHS_OAS2.
ExpressionAtlasiP29728. baseline and differential.
GenevestigatoriP29728.

Organism-specific databases

HPAiCAB024984.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi110993. 2 interactions.
STRINGi9606.ENSP00000342278.

Structurei

3D structure databases

ProteinModelPortaliP29728.
SMRiP29728. Positions 8-336, 340-680.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 335325OAS domain 1Add
BLAST
Regioni343 – 683341OAS domain 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi326 – 34621Pro-rich (linker)Add
BLAST

Sequence similaritiesi

Belongs to the 2-5A synthase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG124087.
GeneTreeiENSGT00510000046406.
HOGENOMiHOG000013200.
HOVERGENiHBG007855.
KOiK14216.
OMAiKSYTSQK.
OrthoDBiEOG7WDN1R.
PhylomeDBiP29728.
TreeFamiTF329749.

Family and domain databases

Gene3Di1.10.1410.20. 2 hits.
InterProiIPR006117. 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]
PANTHERiPTHR11258. PTHR11258. 1 hit.
PfamiPF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 2 hits.
[Graphical view]
PROSITEiPS00832. 25A_SYNTH_1. 2 hits.
PS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform p71 (identifier: P29728-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGNGESQLSS VPAQKLGWFI QEYLKPYEEC QTLIDEMVNT ICDVLQEPEQ
60 70 80 90 100
FPLVQGVAIG GSYGRKTVLR GNSDGTLVLF FSDLKQFQDQ KRSQRDILDK
110 120 130 140 150
TGDKLKFCLF TKWLKNNFEI QKSLDGFTIQ VFTKNQRISF EVLAAFNALS
160 170 180 190 200
LNDNPSPWIY RELKRSLDKT NASPGEFAVC FTELQQKFFD NRPGKLKDLI
210 220 230 240 250
LLIKHWHQQC QKKIKDLPSL SPYALELLTV YAWEQGCRKD NFDIAEGVRT
260 270 280 290 300
VLELIKCQEK LCIYWMVNYN FEDETIRNIL LHQLQSARPV ILDPVDPTNN
310 320 330 340 350
VSGDKICWQW LKKEAQTWLT SPNLDNELPA PSWNVLPAPL FTTPGHLLDK
360 370 380 390 400
FIKEFLQPNK CFLEQIDSAV NIIRTFLKEN CFRQSTAKIQ IVRGGSTAKG
410 420 430 440 450
TALKTGSDAD LVVFHNSLKS YTSQKNERHK IVKEIHEQLK AFWREKEEEL
460 470 480 490 500
EVSFEPPKWK APRVLSFSLK SKVLNESVSF DVLPAFNALG QLSSGSTPSP
510 520 530 540 550
EVYAGLIDLY KSSDLPGGEF STCFTVLQRN FIRSRPTKLK DLIRLVKHWY
560 570 580 590 600
KECERKLKPK GSLPPKYALE LLTIYAWEQG SGVPDFDTAE GFRTVLELVT
610 620 630 640 650
QYQQLCIFWK VNYNFEDETV RKFLLSQLQK TRPVILDPAE PTGDVGGGDR
660 670 680 690 700
WCWHLLAKEA KEWLSSPCFK DGTGNPIPPW KVPTMQTPGS CGARIHPIVN
710
EMFSSRSHRI LNNNSKRNF
Length:719
Mass (Da):82,431
Last modified:January 23, 2007 - v3
Checksum:i1B680D397D5EDB78
GO
Isoform p69 (identifier: P29728-2) [UniParc]FASTAAdd to Basket

Also known as: 69 kDa

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

Show »
Length:687
Mass (Da):78,787
Checksum:i34729B5A88A38B2D
GO
Isoform 3 (identifier: P29728-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     151-172: LNDNPSPWIYRELKRSLDKTNA → KHCWVSGEKSQRSGCQTALCNL
     173-719: Missing.

Note: No experimental confirmation available.

Show »
Length:172
Mass (Da):19,517
Checksum:i8CF5C0C9EE9850A9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 473LQE → CRN in AAA60607. (PubMed:1577824)Curated
Sequence conflicti45 – 473LQE → CRN in AAA60606. (PubMed:1577824)Curated
Sequence conflicti127 – 1271F → S in AAA60607. (PubMed:1577824)Curated
Sequence conflicti127 – 1271F → S in AAA60606. (PubMed:1577824)Curated
Sequence conflicti606 – 6061C → G in AAA60607. (PubMed:1577824)Curated
Sequence conflicti606 – 6061C → G in AAA60606. (PubMed:1577824)Curated
Sequence conflicti639 – 6391A → G in AAA60607. (PubMed:1577824)Curated
Sequence conflicti639 – 6391A → G in AAA60606. (PubMed:1577824)Curated
Sequence conflicti657 – 6571A → D in AAA60607. (PubMed:1577824)Curated
Sequence conflicti657 – 6571A → D in AAA60606. (PubMed:1577824)Curated
Sequence conflicti662 – 6632EW → VR in AAA60607. (PubMed:1577824)Curated
Sequence conflicti662 – 6632EW → VR in AAA60606. (PubMed:1577824)Curated
Sequence conflicti719 – 7191F → FWRSSGNRF in AAA60607. (PubMed:1577824)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei151 – 17222LNDNP…DKTNA → KHCWVSGEKSQRSGCQTALC NL in isoform 3. 1 PublicationVSP_043354Add
BLAST
Alternative sequencei173 – 719547Missing in isoform 3. 1 PublicationVSP_043355Add
BLAST
Alternative sequencei684 – 6874TMQT → VKVI in isoform p69. 3 PublicationsVSP_003741
Alternative sequencei688 – 71932Missing in isoform p69. 3 PublicationsVSP_003742Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31906.1. [P29728-1]
CCDS41839.1. [P29728-2]
CCDS44982.1. [P29728-3]
PIRiB42665.
RefSeqiNP_001027903.1. NM_001032731.1. [P29728-3]
NP_002526.2. NM_002535.2. [P29728-2]
NP_058197.2. NM_016817.2. [P29728-1]
UniGeneiHs.414332.

Genome annotation databases

EnsembliENST00000342315; ENSP00000342278; ENSG00000111335. [P29728-1]
ENST00000392583; ENSP00000376362; ENSG00000111335. [P29728-2]
ENST00000449768; ENSP00000411763; ENSG00000111335. [P29728-3]
GeneIDi4939.
KEGGihsa:4939.
UCSCiuc001tuh.3. human. [P29728-3]
uc001tui.1. human. [P29728-2]
uc001tuj.3. human. [P29728-1]

Polymorphism databases

DMDMi116242687.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS31906.1. [P29728-1 ]
CCDS41839.1. [P29728-2 ]
CCDS44982.1. [P29728-3 ]
PIRi B42665.
RefSeqi NP_001027903.1. NM_001032731.1. [P29728-3 ]
NP_002526.2. NM_002535.2. [P29728-2 ]
NP_058197.2. NM_016817.2. [P29728-1 ]
UniGenei Hs.414332.

3D structure databases

ProteinModelPortali P29728.
SMRi P29728. Positions 8-336, 340-680.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110993. 2 interactions.
STRINGi 9606.ENSP00000342278.

PTM databases

PhosphoSitei P29728.

Polymorphism databases

DMDMi 116242687.

Proteomic databases

MaxQBi P29728.
PaxDbi P29728.
PRIDEi P29728.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000342315 ; ENSP00000342278 ; ENSG00000111335 . [P29728-1 ]
ENST00000392583 ; ENSP00000376362 ; ENSG00000111335 . [P29728-2 ]
ENST00000449768 ; ENSP00000411763 ; ENSG00000111335 . [P29728-3 ]
GeneIDi 4939.
KEGGi hsa:4939.
UCSCi uc001tuh.3. human. [P29728-3 ]
uc001tui.1. human. [P29728-2 ]
uc001tuj.3. human. [P29728-1 ]

Organism-specific databases

CTDi 4939.
GeneCardsi GC12P113416.
H-InvDB HIX0129679.
HGNCi HGNC:8087. OAS2.
HPAi CAB024984.
MIMi 603350. gene.
neXtProti NX_P29728.
PharmGKBi PA31876.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG124087.
GeneTreei ENSGT00510000046406.
HOGENOMi HOG000013200.
HOVERGENi HBG007855.
KOi K14216.
OMAi KSYTSQK.
OrthoDBi EOG7WDN1R.
PhylomeDBi P29728.
TreeFami TF329749.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000111335-MONOMER.
Reactomei REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.

Miscellaneous databases

GeneWikii OAS2.
GenomeRNAii 4939.
NextBioi 19027.
PROi P29728.
SOURCEi Search...

Gene expression databases

Bgeei P29728.
CleanExi HS_OAS2.
ExpressionAtlasi P29728. baseline and differential.
Genevestigatori P29728.

Family and domain databases

Gene3Di 1.10.1410.20. 2 hits.
InterProi 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 ]
PANTHERi PTHR11258. PTHR11258. 1 hit.
Pfami PF01909. NTP_transf_2. 1 hit.
PF10421. OAS1_C. 2 hits.
[Graphical view ]
PROSITEi PS00832. 25A_SYNTH_1. 2 hits.
PS00833. 25A_SYNTH_2. 2 hits.
PS50152. 25A_SYNTH_3. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiOAS2_HUMAN
AccessioniPrimary (citable) accession number: P29728
Secondary accession number(s): A8K9T1, Q6PJ33, Q86XX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3