P17181 (INAR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interferon alpha/beta receptor 1
Short name=IFN-R-1
Short name=IFN-alpha/beta receptor 1

Alternative name(s):
Cytokine receptor class-II member 1
Cytokine receptor family 2 member 1
Short name=CRF2-1
Type I interferon receptor 1

Gene names

Name:	IFNAR1
Synonyms:	IFNAR

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	557 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 IFNAR2 to form the type I interferon receptor. Receptor for interferons alpha and beta. Binding to type I IFNs triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and IFNR alpha- and beta-subunits themselves.
Subunit structure	Heterodimer with IFNAR2; in presence of interferon alpha and beta ligands, the heterodimer forms the type I interferon receptor. Interacts with STAT1 and STAT2; the interaction requires its phosphorylation at Tyr-466. Interacts with IFNAR2. Ref.11 Ref.12
Subcellular location	Isoform 1: Membrane; Single-pass type I membrane protein.
Tissue specificity	IFN receptors are present in all tissues and even on the surface of most IFN-resistant cells. Isoform 1, isoform 2 and isoform 3 are expressed in the IFN-alpha sensitive myeloma cell line U266B1. Isoform 2 and isoform 3 are expressed in the IFN-alpha resistant myeloma cell line U266R. Isoform 1 is not expressed in IFN-alpha resistant myeloma cell line U266R. Ref.9
Post-translational modification	Phosphorylated on tyrosine residues by TYK2 tyrosine kinase. Ref.10 Palmitoylation at Cys-463 is required for the activation of STAT1 and STAT2. Ref.13
Sequence similarities	Belongs to the type II cytokine receptor family. Contains 3 fibronectin type-III domains.
Sequence caution	The sequence AAH02590.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade Traceable author statement PubMed 7665574. Source: ProtInc T cell activation Inferred from electronic annotation. Source: Compara defense response to virus Inferred from electronic annotation. Source: Compara positive regulation of interferon-gamma production Inferred from electronic annotation. Source: Compara regulation of type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome response to virus Traceable author statement Ref.1. Source: ProtInc type I interferon biosynthetic process Inferred from electronic annotation. Source: Compara type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular_component	integral to plasma membrane Traceable author statement PubMed 8181059. Source: ProtInc
Molecular_function	type I interferon receptor activity Traceable author statement PubMed 7665574. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P17181-1)

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 2 (identifier: P17181-2)

Also known as: Sol-1; Soluble form 1;

The sequence of this isoform differs from the canonical sequence as follows:
     428-434: KTKPGNT → NISLNSH
     435-557: Missing.

Note: Incomplete sequence.

Isoform 3 (identifier: P17181-3)

Also known as: Sol-2; Soluble form 2;

The sequence of this isoform differs from the canonical sequence as follows:
     414-421: Missing.
     428-480: Missing.

Note: Incomplete sequence.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Potential

Chain

28 – 557

530

Interferon alpha/beta receptor 1

PRO_0000011001

Regions

Topological domain

28 – 436

409

Extracellular Potential

Transmembrane

437 – 457

21

Helical; Potential

Topological domain

458 – 557

100

Cytoplasmic Potential

Domain

134 – 224

91

Fibronectin type-III 1

Domain

230 – 326

97

Fibronectin type-III 2

Domain

334 – 425

92

Fibronectin type-III 3

Amino acid modifications

Modified residue

466

1

Phosphotyrosine; by TYK2 Probable

Modified residue

481

1

Phosphotyrosine; by TYK2 Probable

Modified residue

495

1

Phosphoserine Ref.15

Lipidation

463

1

S-palmitoyl cysteine Ref.13

Glycosylation

50

1

N-linked (GlcNAc...) Potential

Glycosylation

58

1

N-linked (GlcNAc...) Ref.14

Glycosylation

81

1

N-linked (GlcNAc...) Potential

Glycosylation

88

1

N-linked (GlcNAc...) Potential

Glycosylation

110

1

N-linked (GlcNAc...) Ref.14

Glycosylation

172

1

N-linked (GlcNAc...) Ref.16

Glycosylation

254

1

N-linked (GlcNAc...) Potential

Glycosylation

313

1

N-linked (GlcNAc...) Ref.14

Glycosylation

314

1

N-linked (GlcNAc...) Potential

Glycosylation

376

1

N-linked (GlcNAc...) Potential

Glycosylation

416

1

N-linked (GlcNAc...) Potential

Glycosylation

433

1

N-linked (GlcNAc...) Potential

Disulfide bond

79 ↔ 87

Ref.16

Disulfide bond

199 ↔ 220

Ref.16

Disulfide bond

283 ↔ 291

Ref.16

Natural variations

Alternative sequence

414 – 421

8

Missing in isoform 3.

VSP_029928

Alternative sequence

428 – 480

53

Missing in isoform 3.

VSP_029929

Alternative sequence

428 – 434

7

KTKPGNT → NISLNSH in isoform 2.

VSP_029930

Alternative sequence

435 – 557

123

Missing in isoform 2.

VSP_029931

Natural variant

168

1

V → L. Ref.1 Ref.2 Ref.4
Corresponds to variant rs2257167 [ dbSNP | Ensembl ].

VAR_002717

Natural variant

307

1

V → I. Ref.5
Corresponds to variant rs17875833 [ dbSNP | Ensembl ].

VAR_020502

Natural variant

359

1

T → M. Ref.5
Corresponds to variant rs17875834 [ dbSNP | Ensembl ].

VAR_020503

Experimental info

Sequence conflict

17

1

A → G in AAA52730. Ref.1

Sequence conflict

59

1

V → M in BAD96532. Ref.4

Sequence conflict

279

1

Q → R in BAD96532. Ref.4

Sequence conflict

344

1

D → G in BAG35516. Ref.3

Sequence conflict

479

1

D → N in BAD96532. Ref.4

Secondary structure

1

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557

Helix Strand Turn

Details...

Beta strand

37 – 41

5

Beta strand

44 – 48

5

Beta strand

60 – 69

10

Beta strand

80 – 88

9

Beta strand

100 – 107

8

Beta strand

112 – 116

5

Helix

122 – 125

4

Beta strand

132 – 137

6

Beta strand

142 – 147

6

Beta strand

164 – 171

8

Turn

172 – 174

3

Beta strand

178 – 183

6

Beta strand

186 – 189

4

Beta strand

197 – 206

10

Helix

207 – 209

3

Beta strand

219 – 222

4

Beta strand

233 – 240

8

Beta strand

243 – 249

7

Beta strand

251 – 254

4

Beta strand

256 – 263

8

Helix

264 – 267

4

Helix

281 – 283

3

Beta strand

286 – 294

9

Helix

295 – 297

3

Beta strand

300 – 310

11

Beta strand

322 – 325

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 3. Checksum: 24A01779DB7F356F	FASTA	557	63,525
	10 20 30 40 50 60 MMVVLLGATT LVLVAVAPWV LSAAAGGKNL KSPQKVEVDI IDDNFILRWN RSDESVGNVT 70 80 90 100 110 120 FSFDYQKTGM DNWIKLSGCQ NITSTKCNFS SLKLNVYEEI KLRIRAEKEN TSSWYEVDSF 130 140 150 160 170 180 TPFRKAQIGP PEVHLEAEDK AIVIHISPGT KDSVMWALDG LSFTYSLVIW KNSSGVEERI 190 200 210 220 230 240 ENIYSRHKIY KLSPETTYCL KVKAALLTSW KIGVYSPVHC IKTTVENELP PPENIEVSVQ 250 260 270 280 290 300 NQNYVLKWDY TYANMTFQVQ WLHAFLKRNP GNHLYKWKQI PDCENVKTTQ CVFPQNVFQK 310 320 330 340 350 360 GIYLLRVQAS DGNNTSFWSE EIKFDTEIQA FLLPPVFNIR SLSDSFHIYI GAPKQSGNTP 370 380 390 400 410 420 VIQDYPLIYE IIFWENTSNA ERKIIEKKTD VTVPNLKPLT VYCVKARAHT MDEKLNKSSV 430 440 450 460 470 480 FSDAVCEKTK PGNTSKIWLI VGICIALFAL PFVIYAAKVF LRCINYVFFP SLKPSSSIDE 490 500 510 520 530 540 YFSEQPLKNL LLSTSEEQIE KCFIIENIST IATVEETNQT DEDHKKYSSQ TSQDSGNYSN 550 EDESESKTSE ELQQDFV
	Isoform 2 (Sol-1) (Soluble form 1) [UniParc]. Checksum: 4744EF06968FD2EA	FASTA	434	49,547
	10 20 30 40 50 60 MMVVLLGATT LVLVAVAPWV LSAAAGGKNL KSPQKVEVDI IDDNFILRWN RSDESVGNVT 70 80 90 100 110 120 FSFDYQKTGM DNWIKLSGCQ NITSTKCNFS SLKLNVYEEI KLRIRAEKEN TSSWYEVDSF 130 140 150 160 170 180 TPFRKAQIGP PEVHLEAEDK AIVIHISPGT KDSVMWALDG LSFTYSLVIW KNSSGVEERI 190 200 210 220 230 240 ENIYSRHKIY KLSPETTYCL KVKAALLTSW KIGVYSPVHC IKTTVENELP PPENIEVSVQ 250 260 270 280 290 300 NQNYVLKWDY TYANMTFQVQ WLHAFLKRNP GNHLYKWKQI PDCENVKTTQ CVFPQNVFQK 310 320 330 340 350 360 GIYLLRVQAS DGNNTSFWSE EIKFDTEIQA FLLPPVFNIR SLSDSFHIYI GAPKQSGNTP 370 380 390 400 410 420 VIQDYPLIYE IIFWENTSNA ERKIIEKKTD VTVPNLKPLT VYCVKARAHT MDEKLNKSSV 430 FSDAVCENIS LNSH
	Isoform 3 (Sol-2) (Soluble form 2) [UniParc]. Checksum: 16984A61FE2BF41C	FASTA	496	56,718
	10 20 30 40 50 60 MMVVLLGATT LVLVAVAPWV LSAAAGGKNL KSPQKVEVDI IDDNFILRWN RSDESVGNVT 70 80 90 100 110 120 FSFDYQKTGM DNWIKLSGCQ NITSTKCNFS SLKLNVYEEI KLRIRAEKEN TSSWYEVDSF 130 140 150 160 170 180 TPFRKAQIGP PEVHLEAEDK AIVIHISPGT KDSVMWALDG LSFTYSLVIW KNSSGVEERI 190 200 210 220 230 240 ENIYSRHKIY KLSPETTYCL KVKAALLTSW KIGVYSPVHC IKTTVENELP PPENIEVSVQ 250 260 270 280 290 300 NQNYVLKWDY TYANMTFQVQ WLHAFLKRNP GNHLYKWKQI PDCENVKTTQ CVFPQNVFQK 310 320 330 340 350 360 GIYLLRVQAS DGNNTSFWSE EIKFDTEIQA FLLPPVFNIR SLSDSFHIYI GAPKQSGNTP 370 380 390 400 410 420 VIQDYPLIYE IIFWENTSNA ERKIIEKKTD VTVPNLKPLT VYCVKARAHT MDESDAVCEY 430 440 450 460 470 480 FSEQPLKNLL LSTSEEQIEK CFIIENISTI ATVEETNQTD EDHKKYSSQT SQDSGNYSNE 490 DESESKTSEE LQQDFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic transfer of a functional human interferon alpha receptor into mouse cells: cloning and expression of its cDNA." Uze G., Lutfalla G., Gresser I. Cell 60:225-234(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-168.
[2]	"The structure of the human interferon alpha/beta receptor gene." Lutfalla G., Gardiner K., Proudhon D., Vielh E., Uze G. J. Biol. Chem. 267:2802-2809(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-168.
[3]	"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].
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-168. Tissue: Liver.
[5]	SeattleSNPs variation discovery resource Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-307 AND MET-359.
[6]	"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].
[7]	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].
[8]	"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 1). Tissue: Brain and Ovary.
[9]	"Identification of mRNAs encoding two different soluble forms of the human interferon alpha-receptor." Abramovich C., Ratovitski E., Lundgren E., Revel M. FEBS Lett. 338:295-300(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 398-514 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 419-557 (ISOFORM 2), TISSUE SPECIFICITY, ALTERNATIVE SPLICING. Tissue: Myeloma.
[10]	"Direct binding to and tyrosine phosphorylation of the alpha subunit of the type I interferon receptor by p135tyk2 tyrosine kinase." Colamonici O., Yan H., Domanski P., Handa R., Smalley D., Mullersman J., Witte M., Krishnan K., Krolewski J. Mol. Cell. Biol. 14:8133-8142(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY TYK2.
[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 IFNAR2.
[13]	"Palmitoylation of interferon-alpha (IFN-alpha) receptor subunit IFNAR1 is required for the activation of Stat1 and Stat2 by IFN-alpha." Claudinon J., Gonnord P., Beslard E., Marchetti M., Mitchell K., Boularan C., Johannes L., Eid P., Lamaze C. J. Biol. Chem. 284:24328-24340(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-463.
[14]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-58; ASN-110 AND ASN-313, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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 IFNAR2 AND IFNW1, DISULFIDE BONDS, GLYCOSYLATION AT ASN-172.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03171 mRNA. Translation: AAA52730.1.
X60459 Genomic DNA. Translation: CAA42992.1.
AK312631 mRNA. Translation: BAG35516.1.
AK222770 mRNA. Translation: BAD96490.1.
AK222812 mRNA. Translation: BAD96532.1.
AY654286 Genomic DNA. Translation: AAT49100.1.
AF039907 Genomic DNA. No translation available.
AP000296 Genomic DNA. No translation available.
AP000297 Genomic DNA. No translation available.
AP000298 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09837.1.
CH471079 Genomic DNA. Translation: EAX09839.1.
BC002590 mRNA. Translation: AAH02590.1. Sequence problems.
BC021825 mRNA. Translation: AAH21825.1.

IPI

IPI00012877.
IPI00877141.
IPI00877162.

PIR

A32694.
S41602.

RefSeq

NP_000620.2. NM_000629.2.

UniGene

Hs.529400.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3S98	X-ray	1.90	A	30-332	[»]
3SE3	X-ray	4.00	A	28-436	[»]
3SE4	X-ray	3.50	A	28-436	[»]

ProteinModelPortal

P17181.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-57N.

IntAct

P17181. 5 interactions.

MINT

MINT-107953.

STRING

9606.ENSP00000270139.

PTM databases

PhosphoSite

P17181.

Polymorphism databases

DMDM

90110827.

Proteomic databases

PaxDb

P17181.

PRIDE

P17181.

Protocols and materials databases

DNASU

3454.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000270139; ENSP00000270139; ENSG00000142166.

GeneID

3454.

KEGG

hsa:3454.

UCSC

uc002yrn.3. human.

Organism-specific databases

CTD

3454.

GeneCards

GC21P034696.

HGNC

HGNC:5432. IFNAR1.

HPA

HPA018015.

MIM

107450. gene.

neXtProt

NX_P17181.

PharmGKB

PA29670.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG43815.

HOVERGEN

HBG052126.

InParanoid

P17181.

KO

K05130.

OMA

TSFWSEE.

OrthoDB

EOG44J2J0.

PhylomeDB

P17181.

Enzyme and pathway databases

Pathway_Interaction_DB

cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P17181.

Bgee

P17181.

CleanEx

HS_IFNAR1.

Genevestigator

P17181.

GermOnline

ENSG00000142166. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 4 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR016669. Interferon_alpha/beta_rcpt-1.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
[Graphical view]

Pfam

PF09294. Interfer-bind. 2 hits.
[Graphical view]

PIRSF

PIRSF016567. IFN_alpha/beta_recept-1. 1 hit.

SMART

SM00060. FN3. 4 hits.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 4 hits.

PROSITE

PS50853. FN3. False negative.
[Graphical view]

ProtoNet

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ChEMBL

CHEMBL1887.

ChiTaRS

IFNAR1. 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

P17181.

GenomeRNAi

3454.

NextBio

13606.

SOURCE

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Entry information

Entry name

INAR1_HUMAN

Accession

Primary (citable) accession number: P17181
Secondary accession number(s): B2R6L9 , D3DSF0, Q53GW9, Q53H11, Q6PKD7, Q7M4L2, Q8WTZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 127 of the entry and version 3 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.