P48551 (INAR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	515 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade Traceable author statement Ref.2. Source: ProtInc cell proliferation Inferred from electronic annotation. Source: Compara regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara 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-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular_component	extracellular region Traceable author statement Ref.2. Source: ProtInc extracellular space Inferred from direct assay Ref.4. Source: UniProtKB integral to plasma membrane Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	type I interferon receptor activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CREBBP	Q92793	4	EBI-958408,EBI-81215
GNB2L1	P63244	4	EBI-958408,EBI-296739
IRF9	Q00978	6	EBI-958408,EBI-626526
STAT2	P52630	2	EBI-958408,EBI-1546963

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Chain

27 – 515

489

Interferon alpha/beta receptor 2

PRO_0000011006

Regions

Topological domain

27 – 243

217

Extracellular Potential

Transmembrane

244 – 264

21

Helical; Potential

Topological domain

265 – 515

251

Cytoplasmic Potential

Amino acid modifications

Modified residue

400

1

Phosphoserine By similarity

Glycosylation

58

1

N-linked (GlcNAc...) Potential

Glycosylation

87

1

N-linked (GlcNAc...) Ref.1

Glycosylation

116

1

N-linked (GlcNAc...) Potential

Glycosylation

188

1

N-linked (GlcNAc...) Potential

Glycosylation

192

1

N-linked (GlcNAc...) Ref.1

Disulfide bond

39 ↔ 122

Ref.15 Ref.17 Ref.18 Ref.19

Disulfide bond

85 ↔ 93

Ref.15 Ref.17 Ref.18 Ref.19

Disulfide bond

207 ↔ 227

Ref.15 Ref.17 Ref.18 Ref.19

Natural variations

Alternative sequence

238 – 239

2

SA → FS in isoform 3.

VSP_001736

Alternative sequence

240 – 515

276

Missing in isoform 3.

VSP_001737

Alternative sequence

281 – 331

51

NFHNF…EAAPR → RQGLAKGWNAVAIHRCSHNA LQSETPELKQSSCLSFPSSW DYKRASLCPSD in isoform 2.

VSP_001738

Alternative sequence

332 – 515

184

Missing in isoform 2.

VSP_001739

Natural variant

8

1

F → 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 variant

10

1

F → V. Ref.1 Ref.4 Ref.5 Ref.6 Ref.16
Corresponds to variant rs1051393 [ dbSNP | Ensembl ].

VAR_020522

Natural variant

196

1

I → V. Ref.6
Corresponds to variant rs17860223 [ dbSNP | Ensembl ].

VAR_020523

Experimental info

Mutagenesis

269

1

Y → 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

Mutagenesis

306

1

Y → 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

Mutagenesis

316

1

Y → 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

Mutagenesis

318

1

Y → 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

Mutagenesis

337

1

Y → 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

Mutagenesis

411

1

Y → 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

Mutagenesis

512

1

Y → 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 conflict

151

1

M → V in AAC50202. Ref.3

Secondary structure

1

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515

Helix Strand Turn

Details...

Beta strand

40 – 46

7

Beta strand

49 – 55

7

Beta strand

59 – 61

3

Beta strand

65 – 75

11

Helix

83 – 85

3

Beta strand

86 – 89

4

Beta strand

91 – 94

4

Turn

96 – 98

3

Beta strand

102 – 104

3

Beta strand

106 – 113

8

Beta strand

119 – 126

8

Helix

128 – 131

4

Beta strand

138 – 143

6

Beta strand

148 – 153

6

Helix

159 – 161

3

Beta strand

167 – 174

8

Beta strand

177 – 181

5

Turn

186 – 188

3

Beta strand

191 – 197

7

Beta strand

205 – 213

9

Beta strand

226 – 229

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long form beta) (IFNaR2-2) (IFNaR2-1b) [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 4D7730D93AA739F4	FASTA	515	57,759
	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
	Isoform 2 (Short form beta) (IFNaR2-1) (IFNaR2-1a) [UniParc]. Checksum: 6F6A2FD6E7A7449B	FASTA	331	37,393
	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 RQGLAKGWNA VAIHRCSHNA 310 320 330 LQSETPELKQ SSCLSFPSSW DYKRASLCPS D
	Isoform 3 (IFNaR2-3) (IFNaR2-2a) (P40) [UniParc]. Checksum: 705E887E728A4FB6	FASTA	239	27,384
	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 HKPEIKGNMS GNFTYIIDKL IPNTNYCVSV YLEHSDEQAV IKSPLKCTLL PPGQESEFS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X77722 mRNA. Translation: CAA54785.1.
L42243 , L42238, L42239, L42240, L42323, L42241, L42242 Genomic DNA. Translation: AAB46417.1.
L42243 , L42238, L42239, L42240, L42323, L42241 Genomic DNA. Translation: AAB46418.1.
L42243 , 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.

IPI

IPI00010193.
IPI00220690.
IPI00220691.

PIR

I39073.
S59501.

RefSeq

NP_000865.2. NM_000874.3.
NP_997467.1. NM_207584.1.
NP_997468.1. NM_207585.1.

UniGene

Hs.708195.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N6U	NMR	-	A	28-237	[»]
1N6V	NMR	-	A	28-237	[»]
2HYM	NMR	-	A	28-237	[»]
2KZ1	NMR	-	B	28-237	[»]
2LAG	NMR	-	B	28-237	[»]
3S8W	X-ray	2.60	A/B/C	131-232	[»]
3S9D	X-ray	2.00	B/D	37-232	[»]
3SE3	X-ray	4.00	C	34-232	[»]
3SE4	X-ray	3.50	C	34-232	[»]

ProteinModelPortal

P48551.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-945N.

IntAct

P48551. 11 interactions.

MINT

MINT-196715.

STRING

9606.ENSP00000343957.

PTM databases

PhosphoSite

P48551.

Polymorphism databases

DMDM

1352466.

Proteomic databases

PaxDb

P48551.

PRIDE

P48551.

Protocols and materials databases

DNASU

3455.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000342101; ENSP00000343289; ENSG00000159110.
ENST00000342136; ENSP00000343957; ENSG00000159110.
ENST00000382241; ENSP00000371676; ENSG00000159110.
ENST00000382264; ENSP00000371699; ENSG00000159110.
ENST00000404220; ENSP00000384309; ENSG00000159110.

GeneID

3455.

KEGG

hsa:3455.

UCSC

uc002yrb.3. human.
uc002yrd.3. human.
uc002yrf.3. human.

Organism-specific databases

CTD

3455.

GeneCards

GC21P034602.

HGNC

HGNC:5433. IFNAR2.

HPA

CAB025889.

MIM

602376. gene.
610424. phenotype.

neXtProt

NX_P48551.

PharmGKB

PA29671.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41946.

HOGENOM

HOG000013219.

HOVERGEN

HBG053907.

InParanoid

P48551.

KO

K05131.

OMA

RITFNVD.

PhylomeDB

P48551.

Enzyme and pathway databases

Pathway_Interaction_DB

cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
telomerasepathway. Regulation of Telomerase.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P48551.

Bgee

P48551.

CleanEx

HS_IFNAR2.

Genevestigator

P48551.

GermOnline

ENSG00000159110. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
[Graphical view]

Pfam

PF09294. Interfer-bind. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 2 hits.

ProtoNet

Search...

Other

ChEMBL

CHEMBL2005.

ChiTaRS

IFNAR2. human.

DrugBank

DB00034. 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.

EvolutionaryTrace

P48551.

GenomeRNAi

3455.

NextBio

13610.

PMAP-CutDB

Q6FHD7.

SOURCE

Search...

Entry information

Entry name

INAR2_HUMAN

Accession

Primary (citable) accession number: P48551
Secondary accession number(s): A8KAJ4 , D3DSE8, D3DSE9, Q15467, Q6FHD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 137 of the entry and version 1 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.