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P48551 (INAR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon alpha/beta receptor 2

Short name=IFN-R-2
Short name=IFN-alpha binding protein
Short name=IFN-alpha/beta receptor 2
Alternative name(s):
Interferon alpha binding protein
Type I interferon receptor 2
Gene names
Name:IFNAR2
Synonyms:IFNABR, IFNARB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Associates with IFNAR1 to form the type I interferon receptor. Receptor for interferons alpha and beta. Involved in IFN-mediated STAT1, STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase, JAK1. Isoform 3 is a potent inhibitor of type I IFN receptor activity. Ref.1 Ref.3 Ref.4 Ref.13 Ref.14

Subunit structure

Heterodimer with IFNAR1; in presence of interferon alpha and/or beta ligands forms the type I interferon receptor. Isoform 1 interacts with the transcriptional factors STAT1 and STAT2. Interacts with JAK1. Ref.4 Ref.11 Ref.12

Subcellular location

Isoform 1: Membrane; Single-pass type I membrane protein Ref.1 Ref.4.

Isoform 2: Membrane; Single-pass type I membrane protein Ref.1 Ref.4.

Isoform 3: Secreted Ref.1 Ref.4.

Tissue specificity

Isoform 3 is detected in the urine (at protein level). Expressed in blood cells. Expressed in lymphoblastoid and fibrosarcoma cell lines. Ref.1 Ref.2 Ref.4

Post-translational modification

Phosphorylated on tyrosine residues upon interferon binding. Phosphorylation at Tyr-337 or Tyr-512 are sufficient to mediate interferon dependent activation of STAT1, STAT2 and STAT3 leading to antiproliferative effects on many different cell types. Ref.4 Ref.13 Ref.14

Glycosylated. Ref.1

Polymorphism

Genetic variations in IFNAR2 influence susceptibility to hepatitis B virus (HBV) infection [MIM:610424].

Sequence similarities

Belongs to the type II cytokine receptor family.

Ontologies

Keywords
   Cellular componentMembrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Traceable author statement Ref.2. Source: ProtInc

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cell surface receptor signaling pathway

Traceable author statement PubMed 8798579. Source: ProtInc

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of type I interferon-mediated signaling pathway

Traceable author statement. Source: Reactome

response to interferon-alpha

Inferred from direct assay Ref.4. Source: UniProtKB

response to virus

Traceable author statement Ref.2. Source: ProtInc

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentextracellular region

Traceable author statement Ref.2. Source: ProtInc

extracellular space

Inferred from direct assay Ref.4. Source: UniProtKB

integral component of plasma membrane

Inferred from direct assay Ref.4. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionprotein kinase binding

Inferred from physical interaction Ref.4. Source: UniProtKB

type I interferon binding

Inferred from physical interaction Ref.4. Source: UniProtKB

type I interferon receptor activity

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P48551-1)

Also known as: Long form beta; IFNaR2-2; IFNaR2-1b;

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 2 (identifier: P48551-2)

Also known as: Short form beta; IFNaR2-1; IFNaR2-1a;

The sequence of this isoform differs from the canonical sequence as follows:
     281-331: NFHNFLAWPF...SDSDTEAAPR → RQGLAKGWNA...YKRASLCPSD
     332-515: Missing.
Isoform 3 (identifier: P48551-3)

Also known as: IFNaR2-3; IFNaR2-2a; P40;

The sequence of this isoform differs from the canonical sequence as follows:
     238-239: SA → FS
     240-515: Missing.
Note: Soluble receptor.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626
Chain27 – 515489Interferon alpha/beta receptor 2
PRO_0000011006

Regions

Topological domain27 – 243217Extracellular Potential
Transmembrane244 – 26421Helical; Potential
Topological domain265 – 515251Cytoplasmic Potential

Amino acid modifications

Modified residue3371Phosphotyrosine Ref.13 Ref.14
Modified residue4671Phosphoserine By similarity
Modified residue5121Phosphotyrosine Ref.13 Ref.14
Glycosylation581N-linked (GlcNAc...) Potential
Glycosylation871N-linked (GlcNAc...) Ref.1
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation1921N-linked (GlcNAc...) Ref.1
Disulfide bond39 ↔ 122 Ref.15 Ref.17 Ref.18 Ref.19
Disulfide bond85 ↔ 93 Ref.15 Ref.17 Ref.18 Ref.19
Disulfide bond207 ↔ 227 Ref.15 Ref.17 Ref.18 Ref.19

Natural variations

Alternative sequence238 – 2392SA → FS in isoform 3.
VSP_001736
Alternative sequence240 – 515276Missing in isoform 3.
VSP_001737
Alternative sequence281 – 33151NFHNF…EAAPR → RQGLAKGWNAVAIHRCSHNA LQSETPELKQSSCLSFPSSW DYKRASLCPSD in isoform 2.
VSP_001738
Alternative sequence332 – 515184Missing in isoform 2.
VSP_001739
Natural variant81F → S Associated with susceptibility to HVB infection; lower cell surface levels; lower induction of MHC class 1 expression by INF-alpha. Ref.6 Ref.16
Corresponds to variant rs2229207 [ dbSNP | Ensembl ].
VAR_020521
Natural variant101F → V. Ref.1 Ref.4 Ref.5 Ref.6 Ref.16
Corresponds to variant rs1051393 [ dbSNP | Ensembl ].
VAR_020522
Natural variant1961I → V. Ref.6
Corresponds to variant rs17860223 [ dbSNP | Ensembl ].
VAR_020523

Experimental info

Mutagenesis2691Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-306; F-316; F-318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-306; F-316; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-306; F-316; F-318 and F-337. Ref.13 Ref.14
Mutagenesis3061Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-316; F-318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-316; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-316; F-318 and F-337. Ref.13 Ref.14
Mutagenesis3161Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-318 and F-337. Ref.13 Ref.14
Mutagenesis3181Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316 and F-337. Ref.13 Ref.14
Mutagenesis3371Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316 and F-318. Ref.13 Ref.14
Mutagenesis4111Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318; F-337 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Ref.13 Ref.14
Mutagenesis5121Y → F: Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318; F-337 and F-411. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318 and F-411. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-411. Ref.13 Ref.14
Sequence conflict1511M → V in AAC50202. Ref.3

Secondary structure

.......................................... 515
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long form beta) (IFNaR2-2) (IFNaR2-1b) [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 4D7730D93AA739F4

FASTA51557,759
        10         20         30         40         50         60 
MLLSQNAFIF RSLNLVLMVY ISLVFGISYD SPDYTDESCT FKISLRNFRS ILSWELKNHS 

        70         80         90        100        110        120 
IVPTHYTLLY TIMSKPEDLK VVKNCANTTR SFCDLTDEWR STHEAYVTVL EGFSGNTTLF 

       130        140        150        160        170        180 
SCSHNFWLAI DMSFEPPEFE IVGFTNHINV MVKFPSIVEE ELQFDLSLVI EEQSEGIVKK 

       190        200        210        220        230        240 
HKPEIKGNMS GNFTYIIDKL IPNTNYCVSV YLEHSDEQAV IKSPLKCTLL PPGQESESAE 

       250        260        270        280        290        300 
SAKIGGIITV FLIALVLTST IVTLKWIGYI CLRNSLPKVL NFHNFLAWPF PNLPPLEAMD 

       310        320        330        340        350        360 
MVEVIYINRK KKVWDYNYDD ESDSDTEAAP RTSGGGYTMH GLTVRPLGQA SATSTESQLI 

       370        380        390        400        410        420 
DPESEEEPDL PEVDVELPTM PKDSPQQLEL LSGPCERRKS PLQDPFPEED YSSTEGSGGR 

       430        440        450        460        470        480 
ITFNVDLNSV FLRVLDDEDS DDLEAPLMLS SHLEEMVDPE DPDNVQSNHL LASGEGTQPT 

       490        500        510 
FPSPSSEGLW SEDAPSDQSD TSESDVDLGD GYIMR 

« Hide

Isoform 2 (Short form beta) (IFNaR2-1) (IFNaR2-1a) [UniParc].

Checksum: 6F6A2FD6E7A7449B
Show »

FASTA33137,393
Isoform 3 (IFNaR2-3) (IFNaR2-2a) (P40) [UniParc].

Checksum: 705E887E728A4FB6
Show »

FASTA23927,384

References

« Hide 'large scale' references
[1]"The human interferon alpha/beta receptor: characterization and molecular cloning."
Novick D., Cohen B., Rubinstein M.
Cell 77:391-400(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-87 AND ASN-192, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT VAL-10.
Tissue: Monocyte.
[2]"Mutant U5A cells are complemented by an interferon-alpha beta receptor subunit generated by alternative processing of a new member of a cytokine receptor gene cluster."
Lutfalla G., Holland S.J., Cinato E., Monneron D., Reboul J., Rogers N.C., Smith J.M., Stark G.R., Gardiner K., Mogensen K.E., Kerr I.M., Uze G.
EMBO J. 14:5100-5108(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
Tissue: Lymphoblastoma.
[3]"Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling."
Domanski P., Witte M., Kellum M., Rubinstein M., Hackett R., Pitha P., Colamonici O.R.
J. Biol. Chem. 270:21606-21611(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
Tissue: Myeloma.
[4]"Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor."
Novick D., Cohen B., Tal N., Rubinstein M.
J. Leukoc. Biol. 57:712-718(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH JAK1, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, VARIANT VAL-10.
Tissue: Blood.
[5]Cohen B., Kim S.H., Novick D., Rubinstein M.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-10.
Tissue: Blood.
[6]SeattleSNPs variation discovery resource
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-8; VAL-10 AND VAL-196.
[7]"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 1).
Tissue: Uterus.
[8]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[9]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling."
Li X., Leung S., Kerr I.M., Stark G.R.
Mol. Cell. Biol. 17:2048-2056(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STAT1 AND STAT2.
[12]"Formation of a uniquely stable type I interferon receptor complex by interferon beta is dependent upon particular interactions between interferon beta and its receptor and independent of tyrosine phosphorylation."
Russell-Harde D., Wagner T.C., Perez H.D., Croze E.
Biochem. Biophys. Res. Commun. 255:539-544(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IFNAR1.
[13]"Interferon signaling is dependent on specific tyrosines located within the intracellular domain of IFNAR2c. Expression of IFNAR2c tyrosine mutants in U5A cells."
Wagner T.C., Velichko S., Vogel D., Rani M.R., Leung S., Ransohoff R.M., Stark G.R., Perez H.D., Croze E.
J. Biol. Chem. 277:1493-1499(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-337 AND TYR-512, MUTAGENESIS OF TYR-269; TYR-306; TYR-316; TYR-318; TYR-337; TYR-411 AND TYR-512.
[14]"STAT3 activation by type I interferons is dependent on specific tyrosines located in the cytoplasmic domain of interferon receptor chain 2c. Activation of multiple STATS proceeds through the redundant usage of two tyrosine residues."
Velichko S., Wagner T.C., Turkson J., Jove R., Croze E.
J. Biol. Chem. 277:35635-35641(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-337 AND TYR-512, MUTAGENESIS OF TYR-269; TYR-306; TYR-316; TYR-318; TYR-337; TYR-411 AND TYR-512.
[15]"The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding."
Chill J.H., Quadt S.R., Levy R., Schreiber G., Anglister J.
Structure 11:791-802(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 28-237, DISULFIDE BONDS.
[16]"Class II cytokine receptor gene cluster is a major locus for hepatitis B persistence."
Frodsham A.J., Zhang L., Dumpis U., Taib N.A.M., Best S., Durham A., Hennig B.J.W., Hellier S., Knapp S., Wright M., Chiaramonte M., Bell J.I., Graves M., Whittle H.C., Thomas H.C., Thursz M.R., Hill A.V.S.
Proc. Natl. Acad. Sci. U.S.A. 103:9148-9153(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO HBV INFECTION, VARIANTS SER-8 AND VAL-10, CHARACTERIZATION OF VARIANT SER-8.
[17]"Determination of the human type I interferon receptor binding site on human interferon-alpha2 by cross saturation and an NMR-based model of the complex."
Quadt-Akabayov S.R., Chill J.H., Levy R., Kessler N., Anglister J.
Protein Sci. 15:2656-2668(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 28-239 IN COMPLEX WITH IFNA2, DISULFIDE BONDS.
[18]"Intermolecular interactions in a 44 kDa interferon-receptor complex detected by asymmetric reverse-protonation and two-dimensional NOESY."
Nudelman I., Akabayov S.R., Schnur E., Biron Z., Levy R., Xu Y., Yang D., Anglister J.
Biochemistry 49:5117-5133(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 28-239 IN COMPLEX WITH IFNA2, DISULFIDE BONDS.
[19]"Structural linkage between ligand discrimination and receptor activation by type I interferons."
Thomas C., Moraga I., Levin D., Krutzik P.O., Podoplelova Y., Trejo A., Lee C., Yarden G., Vleck S.E., Glenn J.S., Nolan G.P., Piehler J., Schreiber G., Garcia K.C.
Cell 146:621-632(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 28-436 IN COMPLEX WITH IFNAR1 AND IFNW1, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77722 mRNA. Translation: CAA54785.1.
L42243 expand/collapse EMBL AC list , L42238, L42239, L42240, L42323, L42241, L42242 Genomic DNA. Translation: AAB46417.1.
L42243 expand/collapse EMBL AC list , L42238, L42239, L42240, L42323, L42241 Genomic DNA. Translation: AAB46418.1.
L42243 expand/collapse EMBL AC list , L42238, L42239, L42240, L42323, L42241, L42242 Genomic DNA. Translation: AAB46419.1.
L41942 mRNA. Translation: AAB46413.1.
L41943 mRNA. Translation: AAB46414.1.
L41944 mRNA. Translation: AAB46415.1.
U29584 mRNA. Translation: AAC50202.1.
X89814 mRNA. Translation: CAA61940.1.
X89772 mRNA. Translation: CAA61914.1.
AY740397 Genomic DNA. Translation: AAU21038.1.
AK293059 mRNA. Translation: BAF85748.1.
CR541817 mRNA. Translation: CAG46616.1.
AP000292 Genomic DNA. No translation available.
AP000293 Genomic DNA. No translation available.
AP000294 Genomic DNA. No translation available.
AP000295 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09842.1.
CH471079 Genomic DNA. Translation: EAX09843.1.
CH471079 Genomic DNA. Translation: EAX09844.1.
CH471079 Genomic DNA. Translation: EAX09846.1.
PIRI39073.
S59501.
RefSeqNP_000865.2. NM_000874.4.
NP_997467.1. NM_207584.2.
NP_997468.1. NM_207585.2.
UniGeneHs.708195.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N6UNMR-A28-237[»]
1N6VNMR-A28-237[»]
2HYMNMR-A28-237[»]
2KZ1NMR-B28-237[»]
2LAGNMR-B28-237[»]
3S8WX-ray2.60A/B/C131-232[»]
3S9DX-ray2.00B/D37-232[»]
3SE3X-ray4.00C34-232[»]
3SE4X-ray3.50C34-232[»]
ProteinModelPortalP48551.
SMRP48551. Positions 28-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109677. 10 interactions.
DIPDIP-945N.
IntActP48551. 13 interactions.
MINTMINT-196715.
STRING9606.ENSP00000343957.

Chemistry

ChEMBLCHEMBL2364170.
DrugBankDB00034. Interferon Alfa-2a, Recombinant.
DB00105. Interferon Alfa-2b, Recombinant.
DB00011. Interferon alfa-n1.
DB00018. Interferon alfa-n3.
DB00069. Interferon alfacon-1.
DB00068. Interferon beta-1b.
DB00008. Peginterferon alfa-2a.
DB00022. Peginterferon alfa-2b.

PTM databases

PhosphoSiteP48551.

Polymorphism databases

DMDM1352466.

Proteomic databases

PaxDbP48551.
PRIDEP48551.

Protocols and materials databases

DNASU3455.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342101; ENSP00000343289; ENSG00000159110. [P48551-3]
ENST00000342136; ENSP00000343957; ENSG00000159110. [P48551-1]
ENST00000382241; ENSP00000371676; ENSG00000159110. [P48551-1]
ENST00000382264; ENSP00000371699; ENSG00000159110. [P48551-2]
ENST00000404220; ENSP00000384309; ENSG00000159110. [P48551-2]
GeneID3455.
KEGGhsa:3455.
UCSCuc002yrb.3. human. [P48551-2]
uc002yrd.3. human. [P48551-1]
uc002yrf.3. human. [P48551-3]

Organism-specific databases

CTD3455.
GeneCardsGC21P034602.
HGNCHGNC:5433. IFNAR2.
HPACAB025889.
MIM602376. gene.
610424. phenotype.
neXtProtNX_P48551.
PharmGKBPA29671.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41946.
HOGENOMHOG000013219.
HOVERGENHBG053907.
InParanoidP48551.
KOK05131.
OMAAFVEVIH.
PhylomeDBP48551.
TreeFamTF335897.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP48551.

Gene expression databases

ArrayExpressP48551.
BgeeP48551.
CleanExHS_IFNAR2.
GenevestigatorP48551.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
[Graphical view]
PfamPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
ProtoNetSearch...

Other

ChiTaRSIFNAR2. human.
EvolutionaryTraceP48551.
GeneWikiIFNAR2.
GenomeRNAi3455.
NextBio13610.
PMAP-CutDBQ6FHD7.
PROP48551.
SOURCESearch...

Entry information

Entry nameINAR2_HUMAN
AccessionPrimary (citable) accession number: P48551
Secondary accession number(s): A8KAJ4 expand/collapse secondary AC list , D3DSE8, D3DSE9, Q15467, Q6FHD7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 147 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM