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P17181 (INAR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. 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 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length557 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 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. Can also transduce IFNB signals without the help of IFNAR2, and not activating the Jak-STAT pathway.

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.14

Sequence similarities

Belongs to the type II cytokine receptor family.

Contains 4 fibronectin type-III domains.

Sequence caution

The sequence AAH02590.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Traceable author statement PubMed 7665574. Source: ProtInc

T cell activation

Inferred from electronic annotation. Source: Ensembl

cell surface receptor signaling pathway

Traceable author statement PubMed 7665574. Source: ProtInc

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response to virus

Inferred from electronic annotation. Source: Ensembl

positive regulation of interferon-gamma production

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of plasma membrane

Traceable author statement PubMed 8181059. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 12220192PubMed 14532120PubMed 8605876PubMed 9677371. Source: IntAct

type I interferon receptor activity

Traceable author statement PubMed 7665574. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FBXW11Q9UKB18EBI-1547250,EBI-355189
STAT2P526304EBI-1547250,EBI-1546963

Alternative products

This entry describes 4 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.
Isoform 4 (identifier: P17181-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 557530Interferon alpha/beta receptor 1
PRO_0000011001

Regions

Topological domain28 – 436409Extracellular Potential
Transmembrane437 – 45721Helical; Potential
Topological domain458 – 557100Cytoplasmic Potential
Domain32 – 12695Fibronectin type-III 1
Domain127 – 227101Fibronectin type-III 2
Domain231 – 32999Fibronectin type-III 3
Domain331 – 432102Fibronectin type-III 4

Amino acid modifications

Modified residue4661Phosphotyrosine; by TYK2 Probable
Modified residue4811Phosphotyrosine; by TYK2 Probable
Modified residue4951Phosphoserine Ref.16
Lipidation4631S-palmitoyl cysteine Ref.14
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation581N-linked (GlcNAc...) Ref.15
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation1101N-linked (GlcNAc...) Ref.15
Glycosylation1721N-linked (GlcNAc...) Ref.17
Glycosylation2541N-linked (GlcNAc...) Potential
Glycosylation3131N-linked (GlcNAc...) Ref.15
Glycosylation3141N-linked (GlcNAc...) Potential
Glycosylation3761N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential
Disulfide bond79 ↔ 87 Ref.17
Disulfide bond199 ↔ 220 Ref.17
Disulfide bond283 ↔ 291 Ref.17
Disulfide bond403 ↔ 426 By similarity

Natural variations

Alternative sequence1 – 6969Missing in isoform 4.
VSP_055322
Alternative sequence414 – 4218Missing in isoform 3.
VSP_029928
Alternative sequence428 – 48053Missing in isoform 3.
VSP_029929
Alternative sequence428 – 4347KTKPGNT → NISLNSH in isoform 2.
VSP_029930
Alternative sequence435 – 557123Missing in isoform 2.
VSP_029931
Natural variant1681V → L. Ref.1 Ref.2 Ref.4
Corresponds to variant rs2257167 [ dbSNP | Ensembl ].
VAR_002717
Natural variant3071V → I. Ref.5
Corresponds to variant rs17875833 [ dbSNP | Ensembl ].
VAR_020502
Natural variant3591T → M. Ref.5
Corresponds to variant rs17875834 [ dbSNP | Ensembl ].
VAR_020503

Experimental info

Sequence conflict171A → G in AAA52730. Ref.1
Sequence conflict591V → M in BAD96532. Ref.4
Sequence conflict2791Q → R in BAD96532. Ref.4
Sequence conflict3441D → G in BAG35516. Ref.3
Sequence conflict4791D → N in BAD96532. Ref.4

Secondary structure

................................................. 557
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 7, 2006. Version 3.
Checksum: 24A01779DB7F356F

FASTA55763,525
        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 

« Hide

Isoform 2 (Sol-1) (Soluble form 1) [UniParc].

Checksum: 4744EF06968FD2EA
Show »

FASTA43449,547
Isoform 3 (Sol-2) (Soluble form 2) [UniParc].

Checksum: 16984A61FE2BF41C
Show »

FASTA49656,718
Isoform 4 [UniParc].

Checksum: 29AF6E22379E2E7C
Show »

FASTA48856,046

References

« Hide '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. 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] (ISOFORMS 1 AND 4).
Tissue: Lung.
[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. 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].
[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. 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].
[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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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.
[15]"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.
Tissue: Leukemic T-cell.
[16]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03171 mRNA. Translation: AAA52730.1.
X60459 Genomic DNA. Translation: CAA42992.1.
AK298051 mRNA. Translation: BAG60345.1.
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.
CCDSCCDS13624.1. [P17181-1]
PIRA32694.
S41602.
RefSeqNP_000620.2. NM_000629.2. [P17181-1]
UniGeneHs.529400.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3S98X-ray1.90A30-332[»]
3SE3X-ray4.00A28-436[»]
3SE4X-ray3.50A28-436[»]
4PO6X-ray1.99B478-507[»]
ProteinModelPortalP17181.
SMRP17181. Positions 33-433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109676. 13 interactions.
DIPDIP-57N.
IntActP17181. 7 interactions.
MINTMINT-107953.
STRING9606.ENSP00000270139.

Chemistry

ChEMBLCHEMBL1887.
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

PhosphoSiteP17181.

Polymorphism databases

DMDM90110827.

Proteomic databases

PaxDbP17181.
PRIDEP17181.

Protocols and materials databases

DNASU3454.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000270139; ENSP00000270139; ENSG00000142166. [P17181-1]
ENST00000416947; ENSP00000395606; ENSG00000142166.
GeneID3454.
KEGGhsa:3454.
UCSCuc002yrn.3. human. [P17181-1]

Organism-specific databases

CTD3454.
GeneCardsGC21P034696.
HGNCHGNC:5432. IFNAR1.
HPAHPA018015.
MIM107450. gene.
neXtProtNX_P17181.
PharmGKBPA29670.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43815.
HOVERGENHBG052126.
InParanoidP17181.
KOK05130.
OMAVYCVKAR.
OrthoDBEOG73FQMD.
PhylomeDBP17181.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP17181.

Gene expression databases

ArrayExpressP17181.
BgeeP17181.
CleanExHS_IFNAR1.
GenevestigatorP17181.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR016669. Interferon_alpha/beta_rcpt-1.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
[Graphical view]
PfamPF09294. Interfer-bind. 2 hits.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
PIRSFPIRSF016567. IFN_alpha/beta_recept-1. 1 hit.
SMARTSM00060. FN3. 4 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 4 hits.
PROSITEPS50853. FN3. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIFNAR1. human.
EvolutionaryTraceP17181.
GeneWikiIFNAR1.
GenomeRNAi3454.
NextBio13606.
PROP17181.
SOURCESearch...

Entry information

Entry nameINAR1_HUMAN
AccessionPrimary (citable) accession number: P17181
Secondary accession number(s): B2R6L9 expand/collapse secondary AC list , B4DNT3, D3DSF0, Q53GW9, Q53H11, Q6PKD7, Q7M4L2, Q8WTZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 140 of the entry and version 3 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