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Q15646

- OASL_HUMAN

UniProt

Q15646 - OASL_HUMAN

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Protein

2'-5'-oligoadenylate synthase-like protein

Gene

OASL

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

Functioni

Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. Displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L.3 Publications

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. DNA binding Source: UniProtKB
  3. double-stranded RNA binding Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. thyroid hormone receptor binding Source: UniProtKB
  6. transferase activity Source: InterPro

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. negative regulation of viral genome replication Source: UniProtKB
  5. response to virus Source: UniProtKB
  6. type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
2'-5'-oligoadenylate synthase-like protein
Alternative name(s):
2'-5'-OAS-related protein
Short name:
2'-5'-OAS-RP
59 kDa 2'-5'-oligoadenylate synthase-like protein
Thyroid receptor-interacting protein 14
Short name:
TR-interacting protein 14
Short name:
TRIP-14
p59 OASL
Short name:
p59OASL
Gene namesi
Name:OASL
Synonyms:TRIP14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:8090. OASL.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB
  4. nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31879.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 5145132'-5'-oligoadenylate synthase-like proteinPRO_0000160266Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ15646.
PaxDbiQ15646.
PRIDEiQ15646.

PTM databases

PhosphoSiteiQ15646.

Expressioni

Tissue specificityi

Expressed in most tissues, with the highest levels in primary blood Leukocytes and other hematopoietic system tissues, colon, stomach and to some extent in testis.

Inductioni

By type I interferon (IFN) and viruses.2 Publications

Gene expression databases

BgeeiQ15646.
CleanExiHS_OASL.
GenevestigatoriQ15646.

Organism-specific databases

HPAiHPA001474.

Interactioni

Subunit structurei

Specifically interacts with the ligand binding domain of the thyroid receptor (TR). TRIP14 does not require the presence of thyroid hormone for its interaction. Binds MBD1.1 Publication

Protein-protein interaction databases

BioGridi114191. 3 interactions.
IntActiQ15646. 1 interaction.
MINTiMINT-4993190.
STRINGi9606.ENSP00000257570.

Structurei

Secondary structure

1
514
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi434 – 4407Combined sources
Turni441 – 4433Combined sources
Beta strandi444 – 4507Combined sources
Beta strandi452 – 4554Combined sources
Helixi456 – 46611Combined sources
Turni471 – 4733Combined sources
Beta strandi474 – 4785Combined sources
Beta strandi485 – 4884Combined sources
Helixi489 – 4924Combined sources
Beta strandi498 – 5047Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WH3NMR-A434-507[»]
ProteinModelPortaliQ15646.
SMRiQ15646. Positions 6-346, 368-514.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15646.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini354 – 43380Ubiquitin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini434 – 50976Ubiquitin-like 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The ubiquitin-like domains are essential for its antiviral activity.

Sequence similaritiesi

Belongs to the 2-5A synthase family.Curated
Contains 2 ubiquitin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG309765.
GeneTreeiENSGT00510000046406.
HOGENOMiHOG000022614.
HOVERGENiHBG000994.
KOiK14608.
OMAiCFHSFQE.
OrthoDBiEOG7WDN1R.
PhylomeDBiQ15646.
TreeFamiTF329749.

Family and domain databases

Gene3Di1.10.1410.20. 1 hit.
InterProiIPR006117. 2-5-oligoadenylate_synth_CS.
IPR006116. 2-5-oligoadenylate_synth_N.
IPR018952. 2-5-oligoAdlate_synth_1_dom2/C.
IPR026774. 2-5A_synthase.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR11258. PTHR11258. 1 hit.
PfamiPF10421. OAS1_C. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 2 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 2 hits.
PROSITEiPS00832. 25A_SYNTH_1. 1 hit.
PS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[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 p56 (identifier: Q15646-1) [UniParc]FASTAAdd to Basket

Also known as: OASL a

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
MALMQELYST PASRLDSFVA QWLQPHREWK EEVLDAVRTV EEFLRQEHFQ
60 70 80 90 100
GKRGLDQDVR VLKVVKVGSF GNGTVLRSTR EVELVAFLSC FHSFQEAAKH
110 120 130 140 150
HKDVLRLIWK TMWQSQDLLD LGLEDLRMEQ RVPDALVFTI QTRGTAEPIT
160 170 180 190 200
VTIVPAYRAL GPSLPNSQPP PEVYVSLIKA CGGPGNFCPS FSELQRNFVK
210 220 230 240 250
HRPTKLKSLL RLVKHWYQQY VKARSPRANL PPLYALELLT IYAWEMGTEE
260 270 280 290 300
DENFMLDEGF TTVMDLLLEY EVICIYWTKY YTLHNAIIED CVRKQLKKER
310 320 330 340 350
PIILDPADPT LNVAEGYRWD IVAQRASQCL KQDCCYDNRE NPISSWNVKR
360 370 380 390 400
ARDIHLTVEQ RGYPDFNLIV NPYEPIRKVK EKIRRTRGYS GLQRLSFQVP
410 420 430 440 450
GSERQLLSSR CSLAKYGIFS HTHIYLLETI PSEIQVFVKN PDGGSYAYAI
460 470 480 490 500
NPNSFILGLK QQIEDQQGLP KKQQQLEFQG QVLQDWLGLG IYGIQDSDTL
510
ILSKKKGEAL FPAS
Length:514
Mass (Da):59,226
Last modified:May 30, 2000 - v2
Checksum:i4D8BB655D9EA003E
GO
Isoform p30 (identifier: Q15646-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     220-255: YVKARSPRANLPPLYALELLTIYAWEMGTEEDENFM → AHHPGSGRPHPQRGRRVQMGHRCSEGLPVPETGLLL
     256-514: Missing.

Note: No experimental confirmation available.

Show »
Length:255
Mass (Da):29,084
Checksum:iAB54142EF4549492
GO
Isoform 3 (identifier: Q15646-3) [UniParc]FASTAAdd to Basket

Also known as: OASL d

The sequence of this isoform differs from the canonical sequence as follows:
     220-349: Missing.

Note: Has antiviral activity against RNA viruses.

Show »
Length:384
Mass (Da):43,942
Checksum:i7993256048CEFC6D
GO

Sequence cautioni

The sequence AAC41733.1 differs from that shown. Reason: Frameshift at position 386. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 3813HREWK…LDAVR → TGVEGRGARRCA in AAD28541. (PubMed:9826176)CuratedAdd
BLAST
Sequence conflicti26 – 3813HREWK…LDAVR → TGVEGRGARRCA in AAD28542. (PubMed:9826176)CuratedAdd
BLAST
Sequence conflicti89 – 891S → T in AAD28542. (PubMed:9826176)Curated
Sequence conflicti95 – 11319QEAAK…WKTMW → PGGSQASQRCSEADMENHV in AAD28541. (PubMed:9826176)CuratedAdd
BLAST
Sequence conflicti95 – 11319QEAAK…WKTMW → PGGSQASQRCSEADMENHV in AAD28542. (PubMed:9826176)CuratedAdd
BLAST
Sequence conflicti223 – 2231A → S in AAD28541. (PubMed:9826176)Curated
Sequence conflicti317 – 3171Y → I in AAD28541. (PubMed:9826176)Curated
Sequence conflicti321 – 3211I → T in AAD28541. (PubMed:9826176)Curated
Sequence conflicti324 – 3241Q → L in AAD28541. (PubMed:9826176)Curated
Sequence conflicti341 – 3422NP → KG in AAC41733. (PubMed:7776974)Curated
Sequence conflicti407 – 4071L → F in BAG37039. (PubMed:14702039)Curated
Sequence conflicti445 – 4451S → T in AAD28541. (PubMed:9826176)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti341 – 3411N → I.
Corresponds to variant rs35249920 [ dbSNP | Ensembl ].
VAR_053544

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei220 – 349130Missing in isoform 3. 1 PublicationVSP_046572Add
BLAST
Alternative sequencei220 – 25536YVKAR…DENFM → AHHPGSGRPHPQRGRRVQMG HRCSEGLPVPETGLLL in isoform p30. 1 PublicationVSP_003743Add
BLAST
Alternative sequencei256 – 514259Missing in isoform p30. 1 PublicationVSP_003744Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ225089 mRNA. Translation: CAA12396.1.
AF063611 mRNA. Translation: AAD28541.1.
AF063612 mRNA. Translation: AAD28542.1.
JQ792168 mRNA. Translation: AFJ00074.1.
AK314419 mRNA. Translation: BAG37039.1.
AC079602 Genomic DNA. No translation available.
Z93097 Genomic DNA. No translation available.
BC117408 mRNA. Translation: AAI17409.1.
BC117410 mRNA. Translation: AAI17411.1.
L40387 Genomic DNA. Translation: AAC41733.1. Frameshift.
CCDSiCCDS73536.1. [Q15646-3]
CCDS9211.1. [Q15646-1]
CCDS9212.1. [Q15646-2]
RefSeqiNP_001248754.1. NM_001261825.1. [Q15646-3]
NP_003724.1. NM_003733.3. [Q15646-1]
NP_937856.1. NM_198213.2. [Q15646-2]
UniGeneiHs.118633.

Genome annotation databases

EnsembliENST00000257570; ENSP00000257570; ENSG00000135114. [Q15646-1]
ENST00000339275; ENSP00000341125; ENSG00000135114. [Q15646-2]
ENST00000620239; ENSP00000479512; ENSG00000135114. [Q15646-3]
GeneIDi8638.
KEGGihsa:8638.
UCSCiuc001tzj.2. human. [Q15646-1]
uc001tzk.2. human. [Q15646-2]

Polymorphism databases

DMDMi6226835.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ225089 mRNA. Translation: CAA12396.1 .
AF063611 mRNA. Translation: AAD28541.1 .
AF063612 mRNA. Translation: AAD28542.1 .
JQ792168 mRNA. Translation: AFJ00074.1 .
AK314419 mRNA. Translation: BAG37039.1 .
AC079602 Genomic DNA. No translation available.
Z93097 Genomic DNA. No translation available.
BC117408 mRNA. Translation: AAI17409.1 .
BC117410 mRNA. Translation: AAI17411.1 .
L40387 Genomic DNA. Translation: AAC41733.1 . Frameshift.
CCDSi CCDS73536.1. [Q15646-3 ]
CCDS9211.1. [Q15646-1 ]
CCDS9212.1. [Q15646-2 ]
RefSeqi NP_001248754.1. NM_001261825.1. [Q15646-3 ]
NP_003724.1. NM_003733.3. [Q15646-1 ]
NP_937856.1. NM_198213.2. [Q15646-2 ]
UniGenei Hs.118633.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WH3 NMR - A 434-507 [» ]
ProteinModelPortali Q15646.
SMRi Q15646. Positions 6-346, 368-514.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114191. 3 interactions.
IntActi Q15646. 1 interaction.
MINTi MINT-4993190.
STRINGi 9606.ENSP00000257570.

PTM databases

PhosphoSitei Q15646.

Polymorphism databases

DMDMi 6226835.

Proteomic databases

MaxQBi Q15646.
PaxDbi Q15646.
PRIDEi Q15646.

Protocols and materials databases

DNASUi 8638.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000257570 ; ENSP00000257570 ; ENSG00000135114 . [Q15646-1 ]
ENST00000339275 ; ENSP00000341125 ; ENSG00000135114 . [Q15646-2 ]
ENST00000620239 ; ENSP00000479512 ; ENSG00000135114 . [Q15646-3 ]
GeneIDi 8638.
KEGGi hsa:8638.
UCSCi uc001tzj.2. human. [Q15646-1 ]
uc001tzk.2. human. [Q15646-2 ]

Organism-specific databases

CTDi 8638.
GeneCardsi GC12M121459.
H-InvDB HIX0201831.
HGNCi HGNC:8090. OASL.
HPAi HPA001474.
MIMi 603281. gene.
neXtProti NX_Q15646.
PharmGKBi PA31879.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG309765.
GeneTreei ENSGT00510000046406.
HOGENOMi HOG000022614.
HOVERGENi HBG000994.
KOi K14608.
OMAi CFHSFQE.
OrthoDBi EOG7WDN1R.
PhylomeDBi Q15646.
TreeFami TF329749.

Enzyme and pathway databases

Reactomei REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.

Miscellaneous databases

ChiTaRSi OASL. human.
EvolutionaryTracei Q15646.
GeneWikii OASL.
GenomeRNAii 8638.
NextBioi 32383.
PROi Q15646.
SOURCEi Search...

Gene expression databases

Bgeei Q15646.
CleanExi HS_OASL.
Genevestigatori Q15646.

Family and domain databases

Gene3Di 1.10.1410.20. 1 hit.
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.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
PANTHERi PTHR11258. PTHR11258. 1 hit.
Pfami PF10421. OAS1_C. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view ]
SMARTi SM00213. UBQ. 2 hits.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 2 hits.
PROSITEi PS00832. 25A_SYNTH_1. 1 hit.
PS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "p59OASL, a 2'-5' oligoadenylate synthetase like protein: a novel human gene related to the 2'-5' oligoadenylate synthetase family."
    Hartmann R., Olsen H.S., Widder S., Joergensen R., Justesen J.
    Nucleic Acids Res. 26:4121-4127(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P56).
  2. "Molecular cloning and characterization of two related and interferon-induced 56-kDa and 30-kDa proteins highly similar to 2'-5' oligoadenylate synthetase."
    Rebouillat D., Marie I., Hovanessian A.G.
    Eur. J. Biochem. 257:319-330(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P56 AND P30), FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Monocyte.
  3. "Identification of OASL d, a splice variant of human OASL, with antiviral activity."
    Guo X., Li X., Xu Y., Sun T., Yang G., Wu Z., Li E.
    Int. J. Biochem. Cell Biol. 44:1133-1138(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  4. "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 P56).
    Tissue: Mammary gland.
  5. "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].
  6. "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] (ISOFORM P56).
    Tissue: Brain.
  7. "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
    Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
    Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 260-416 (ISOFORM P56).
  8. "Interaction between the 2'-5' oligoadenylate synthetase-like protein p59 OASL and the transcriptional repressor methyl CpG-binding protein 1."
    Andersen J.B., Strandbygaard D.J., Hartmann R., Justesen J.
    Eur. J. Biochem. 271:628-636(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MBD1.
    Tissue: Leukocyte.
  9. "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.
  10. "The p59 oligoadenylate synthetase-like protein possesses antiviral activity that requires the C-terminal ubiquitin-like domain."
    Marques J., Anwar J., Eskildsen-Larsen S., Rebouillat D., Paludan S.R., Sen G., Williams B.R., Hartmann R.
    J. Gen. Virol. 89:2767-2772(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Differential regulation of the OASL and OAS1 genes in response to viral infections."
    Melchjorsen J., Kristiansen H., Christiansen R., Rintahaka J., Matikainen S., Paludan S.R., Hartmann R.
    J. Interferon Cytokine Res. 29:199-207(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  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. "2',5'-Oligoadenylate synthetase-like gene highly induced by hepatitis C virus infection in human liver is inhibitory to viral replication in vitro."
    Ishibashi M., Wakita T., Esumi M.
    Biochem. Biophys. Res. Commun. 392:397-402(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  14. "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.
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "Solution structure of C-terminal ubiquitin-like domain of human 2'-5'-oligoadenylate synthetase-like protein (p59 OASL)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 432-507.

Entry informationi

Entry nameiOASL_HUMAN
AccessioniPrimary (citable) accession number: Q15646
Secondary accession number(s): B2RAZ2
, I1YDD2, O75686, Q17R95, Q9Y6K6, Q9Y6K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: November 26, 2014
This is version 136 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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