Q15646 (OASL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	OASL
Synonyms:	TRIP14

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.8 Ref.11
Subunit structure	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. Ref.6
Subcellular location	Isoform p56: Nucleus › nucleolus. Cytoplasm Ref.2. Isoform p30: Cytoplasm Ref.2.
Tissue specificity	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.
Induction	By type I interferon (IFN) and viruses. Ref.9 Ref.11
Domain	The ubiquitin-like domains are essential for its antiviral activity.
Sequence similarities	Belongs to the 2-5A synthase family. Contains 2 ubiquitin-like domains.
Caution	This is the ortholog of mouse OASL1.
Sequence caution	The sequence AAC41733.1 differs from that shown. Reason: Frameshift at position 386.

Ontologies

Keywords
Biological process	Antiviral defense Immunity Innate immunity
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	defense response to virus Inferred from electronic annotation. Source: UniProtKB-KW interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome negative regulation of viral genome replication Inferred from direct assay Ref.8Ref.11. Source: UniProtKB response to virus Inferred from direct assay Ref.8Ref.11. Source: UniProtKB type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleolus Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro DNA binding Inferred from direct assay Ref.2. Source: UniProtKB double-stranded RNA binding Inferred from direct assay Ref.2. Source: UniProtKB thyroid hormone receptor binding Traceable author statement Ref.5. Source: UniProtKB transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform p56 (identifier: Q15646-1)

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 p30 (identifier: Q15646-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 514

514

2'-5'-oligoadenylate synthase-like protein

PRO_0000160266

Regions

Domain

354 – 433

80

Ubiquitin-like 1

Domain

434 – 509

76

Ubiquitin-like 2

Natural variations

Alternative sequence

220 – 255

36

YVKAR…DENFM → AHHPGSGRPHPQRGRRVQMG HRCSEGLPVPETGLLL in isoform p30.

VSP_003743

Alternative sequence

256 – 514

259

Missing in isoform p30.

VSP_003744

Natural variant

341

1

N → I.
Corresponds to variant rs35249920 [ dbSNP | Ensembl ].

VAR_053544

Experimental info

Sequence conflict

26 – 38

13

HREWK…LDAVR → TGVEGRGARRCA in AAD28541. Ref.2

Sequence conflict

26 – 38

13

HREWK…LDAVR → TGVEGRGARRCA in AAD28542. Ref.2

Sequence conflict

89

1

S → T in AAD28542. Ref.2

Sequence conflict

95 – 113

19

QEAAK…WKTMW → PGGSQASQRCSEADMENHV in AAD28541. Ref.2

Sequence conflict

95 – 113

19

QEAAK…WKTMW → PGGSQASQRCSEADMENHV in AAD28542. Ref.2

Sequence conflict

223

1

A → S in AAD28541. Ref.2

Sequence conflict

317

1

Y → I in AAD28541. Ref.2

Sequence conflict

321

1

I → T in AAD28541. Ref.2

Sequence conflict

324

1

Q → L in AAD28541. Ref.2

Sequence conflict

341 – 342

2

NP → KG in AAC41733. Ref.5

Sequence conflict

445

1

S → T in AAD28541. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

514

Helix Strand Turn

Details...

Beta strand

434 – 440

7

Turn

441 – 443

3

Beta strand

444 – 450

7

Beta strand

452 – 455

4

Helix

456 – 466

11

Turn

471 – 473

3

Beta strand

474 – 478

5

Beta strand

485 – 488

4

Helix

489 – 492

4

Beta strand

498 – 504

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform p56 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 4D8BB655D9EA003E	FASTA	514	59,226
	10 20 30 40 50 60 MALMQELYST PASRLDSFVA QWLQPHREWK EEVLDAVRTV EEFLRQEHFQ GKRGLDQDVR 70 80 90 100 110 120 VLKVVKVGSF GNGTVLRSTR EVELVAFLSC FHSFQEAAKH HKDVLRLIWK TMWQSQDLLD 130 140 150 160 170 180 LGLEDLRMEQ RVPDALVFTI QTRGTAEPIT VTIVPAYRAL GPSLPNSQPP PEVYVSLIKA 190 200 210 220 230 240 CGGPGNFCPS FSELQRNFVK HRPTKLKSLL RLVKHWYQQY VKARSPRANL PPLYALELLT 250 260 270 280 290 300 IYAWEMGTEE DENFMLDEGF TTVMDLLLEY EVICIYWTKY YTLHNAIIED CVRKQLKKER 310 320 330 340 350 360 PIILDPADPT LNVAEGYRWD IVAQRASQCL KQDCCYDNRE NPISSWNVKR ARDIHLTVEQ 370 380 390 400 410 420 RGYPDFNLIV NPYEPIRKVK EKIRRTRGYS GLQRLSFQVP GSERQLLSSR CSLAKYGIFS 430 440 450 460 470 480 HTHIYLLETI PSEIQVFVKN PDGGSYAYAI NPNSFILGLK QQIEDQQGLP KKQQQLEFQG 490 500 510 QVLQDWLGLG IYGIQDSDTL ILSKKKGEAL FPAS
	Isoform p30 [UniParc]. Checksum: AB54142EF4549492	FASTA	255	29,084
	10 20 30 40 50 60 MALMQELYST PASRLDSFVA QWLQPHREWK EEVLDAVRTV EEFLRQEHFQ GKRGLDQDVR 70 80 90 100 110 120 VLKVVKVGSF GNGTVLRSTR EVELVAFLSC FHSFQEAAKH HKDVLRLIWK TMWQSQDLLD 130 140 150 160 170 180 LGLEDLRMEQ RVPDALVFTI QTRGTAEPIT VTIVPAYRAL GPSLPNSQPP PEVYVSLIKA 190 200 210 220 230 240 CGGPGNFCPS FSELQRNFVK HRPTKLKSLL RLVKHWYQQA HHPGSGRPHP QRGRRVQMGH 250 RCSEGLPVPE TGLLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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]	"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.
[5]	"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).
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ225089 mRNA. Translation: CAA12396.1.
AF063611 mRNA. Translation: AAD28541.1.
AF063612 mRNA. Translation: AAD28542.1.
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.

IPI

IPI00018810.
IPI00218116.

RefSeq

NP_003724.1. NM_003733.3.

UniGene

Hs.118633.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WH3	NMR	-	A	434-507	[»]

ProteinModelPortal

Q15646.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15646. 1 interaction.

STRING

9606.ENSP00000257570.

PTM databases

PhosphoSite

Q15646.

Polymorphism databases

DMDM

6226835.

Proteomic databases

PaxDb

Q15646.

PRIDE

Q15646.

Protocols and materials databases

DNASU

8638.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000257570; ENSP00000257570; ENSG00000135114.
ENST00000339275; ENSP00000341125; ENSG00000135114.

GeneID

8638.

KEGG

hsa:8638.

UCSC

uc001tzj.1. human.
uc001tzk.1. human.

Organism-specific databases

CTD

8638.

GeneCards

GC12M121459.

H-InvDB

HIX0201831.

HGNC

HGNC:8090. OASL.

HPA

HPA001474.

MIM

603281. gene.

neXtProt

NX_Q15646.

PharmGKB

PA31879.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG309765.

HOGENOM

HOG000022614.

HOVERGEN

HBG000994.

InParanoid

Q15646.

KO

K14608.

OMA

IQVFVKN.

OrthoDB

EOG4M0F1G.

PhylomeDB

Q15646.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

Bgee

Q15646.

CleanEx

HS_OASL.

Genevestigator

Q15646.

GermOnline

ENSG00000135114. Homo sapiens.

Family and domain databases

Gene3D

1.10.1410.20. 1 hit.

InterPro

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.
IPR019955. Ubiquitin_supergroup.
[Graphical view]

PANTHER

PTHR11258. PTHR11258. 1 hit.

Pfam

PF10421. OAS1_C. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]

SMART

SM00213. UBQ. 2 hits.
[Graphical view]

PROSITE

PS00832. 25A_SYNTH_1. 1 hit.
PS00833. 25A_SYNTH_2. 1 hit.
PS50152. 25A_SYNTH_3. 1 hit.
PS00299. UBIQUITIN_1. False negative.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

OASL. human.

EvolutionaryTrace

Q15646.

GenomeRNAi

8638.

NextBio

32383.

SOURCE

Search...

Entry information

Entry name

OASL_HUMAN

Accession

Primary (citable) accession number: Q15646
Secondary accession number(s): O75686 , Q17R95, Q9Y6K6, Q9Y6K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 118 of the entry and version 2 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.