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P48551

- INAR2_HUMAN

UniProt

P48551 - INAR2_HUMAN

Protein

Interferon alpha/beta receptor 2

Gene

IFNAR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    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.5 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein kinase binding Source: UniProtKB
    3. type I interferon binding Source: UniProtKB
    4. type I interferon receptor activity Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: Ensembl
    2. cell surface receptor signaling pathway Source: ProtInc
    3. cytokine-mediated signaling pathway Source: Reactome
    4. JAK-STAT cascade Source: ProtInc
    5. regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. regulation of type I interferon-mediated signaling pathway Source: Reactome
    7. response to interferon-alpha Source: UniProtKB
    8. response to virus Source: ProtInc
    9. type I interferon signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Enzyme and pathway databases

    ReactomeiREACT_25162. Interferon alpha/beta signaling.
    REACT_25216. Regulation of IFNA signaling.
    SignaLinkiP48551.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:IFNAR2
    Synonyms:IFNABR, IFNARB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:5433. IFNAR2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: ProtInc
    2. extracellular space Source: UniProtKB
    3. integral component of plasma membrane Source: UniProtKB
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi269 – 2691Y → 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. 2 Publications
    Mutagenesisi306 – 3061Y → 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. 2 Publications
    Mutagenesisi316 – 3161Y → 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. 2 Publications
    Mutagenesisi318 – 3181Y → 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. 2 Publications
    Mutagenesisi337 – 3371Y → 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. 2 Publications
    Mutagenesisi411 – 4111Y → 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. 2 Publications
    Mutagenesisi512 – 5121Y → 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. 2 Publications

    Organism-specific databases

    MIMi610424. phenotype.
    PharmGKBiPA29671.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Add
    BLAST
    Chaini27 – 515489Interferon alpha/beta receptor 2PRO_0000011006Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi39 ↔ 122
    Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi85 ↔ 93
    Glycosylationi87 – 871N-linked (GlcNAc...)1 Publication
    Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi192 – 1921N-linked (GlcNAc...)1 Publication
    Disulfide bondi207 ↔ 227
    Modified residuei337 – 3371Phosphotyrosine3 Publications
    Modified residuei467 – 4671PhosphoserineBy similarity
    Modified residuei512 – 5121Phosphotyrosine3 Publications

    Post-translational modificationi

    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.3 Publications
    Glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP48551.
    PaxDbiP48551.
    PRIDEiP48551.

    PTM databases

    PhosphoSiteiP48551.

    Miscellaneous databases

    PMAP-CutDBQ6FHD7.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP48551.
    BgeeiP48551.
    CleanExiHS_IFNAR2.
    GenevestigatoriP48551.

    Organism-specific databases

    HPAiCAB025889.

    Interactioni

    Subunit structurei

    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 JAK1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CREBBPQ927934EBI-958408,EBI-81215
    GNB2L1P632444EBI-958408,EBI-296739
    IRF9Q009786EBI-958408,EBI-626526
    JAK1P234583EBI-958408,EBI-1383438
    STAT2P526302EBI-958408,EBI-1546963
    USP18Q9UMW84EBI-958408,EBI-356206

    Protein-protein interaction databases

    BioGridi109677. 10 interactions.
    DIPiDIP-945N.
    IntActiP48551. 13 interactions.
    MINTiMINT-196715.
    STRINGi9606.ENSP00000343957.

    Structurei

    Secondary structure

    1
    515
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 467
    Beta strandi49 – 557
    Beta strandi59 – 613
    Beta strandi65 – 7511
    Helixi83 – 853
    Beta strandi86 – 894
    Beta strandi91 – 944
    Turni96 – 983
    Beta strandi102 – 1043
    Beta strandi106 – 1138
    Beta strandi119 – 1268
    Helixi128 – 1314
    Beta strandi138 – 1436
    Beta strandi148 – 1536
    Helixi159 – 1613
    Beta strandi167 – 1748
    Beta strandi177 – 1815
    Turni186 – 1883
    Beta strandi191 – 1977
    Beta strandi205 – 2139
    Beta strandi226 – 2294

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP48551.
    SMRiP48551. Positions 28-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48551.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 243217ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini265 – 515251CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei244 – 26421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the type II cytokine receptor family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG41946.
    HOGENOMiHOG000013219.
    HOVERGENiHBG053907.
    InParanoidiP48551.
    KOiK05131.
    OMAiIYIRLER.
    PhylomeDBiP48551.
    TreeFamiTF335897.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR015373. Interferon_alpha/beta_rcpt_bsu.
    [Graphical view]
    PfamiPF09294. Interfer-bind. 1 hit.
    PF01108. Tissue_fac. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 2 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P48551-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MLLSQNAFIF RSLNLVLMVY ISLVFGISYD SPDYTDESCT FKISLRNFRS    50
    ILSWELKNHS IVPTHYTLLY TIMSKPEDLK VVKNCANTTR SFCDLTDEWR 100
    STHEAYVTVL EGFSGNTTLF SCSHNFWLAI DMSFEPPEFE IVGFTNHINV 150
    MVKFPSIVEE ELQFDLSLVI EEQSEGIVKK HKPEIKGNMS GNFTYIIDKL 200
    IPNTNYCVSV YLEHSDEQAV IKSPLKCTLL PPGQESESAE SAKIGGIITV 250
    FLIALVLTST IVTLKWIGYI CLRNSLPKVL NFHNFLAWPF PNLPPLEAMD 300
    MVEVIYINRK KKVWDYNYDD ESDSDTEAAP RTSGGGYTMH GLTVRPLGQA 350
    SATSTESQLI DPESEEEPDL PEVDVELPTM PKDSPQQLEL LSGPCERRKS 400
    PLQDPFPEED YSSTEGSGGR ITFNVDLNSV FLRVLDDEDS DDLEAPLMLS 450
    SHLEEMVDPE DPDNVQSNHL LASGEGTQPT FPSPSSEGLW SEDAPSDQSD 500
    TSESDVDLGD GYIMR 515
    Length:515
    Mass (Da):57,759
    Last modified:February 1, 1996 - v1
    Checksum:i4D7730D93AA739F4
    GO
    Isoform 2 (identifier: P48551-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:331
    Mass (Da):37,393
    Checksum:i6F6A2FD6E7A7449B
    GO
    Isoform 3 (identifier: P48551-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:239
    Mass (Da):27,384
    Checksum:i705E887E728A4FB6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti151 – 1511M → V in AAC50202. (PubMed:7665574)Curated

    Polymorphismi

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81F → S Associated with susceptibility to HVB infection; lower cell surface levels; lower induction of MHC class 1 expression by INF-alpha. 2 Publications
    Corresponds to variant rs2229207 [ dbSNP | Ensembl ].
    VAR_020521
    Natural varianti10 – 101F → V.5 Publications
    Corresponds to variant rs1051393 [ dbSNP | Ensembl ].
    VAR_020522
    Natural varianti196 – 1961I → V.1 Publication
    Corresponds to variant rs17860223 [ dbSNP | Ensembl ].
    VAR_020523

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei238 – 2392SA → FS in isoform 3. 2 PublicationsVSP_001736
    Alternative sequencei240 – 515276Missing in isoform 3. 2 PublicationsVSP_001737Add
    BLAST
    Alternative sequencei281 – 33151NFHNF…EAAPR → RQGLAKGWNAVAIHRCSHNA LQSETPELKQSSCLSFPSSW DYKRASLCPSD in isoform 2. 3 PublicationsVSP_001738Add
    BLAST
    Alternative sequencei332 – 515184Missing in isoform 2. 3 PublicationsVSP_001739Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13621.1. [P48551-1]
    CCDS13622.1. [P48551-2]
    PIRiI39073.
    S59501.
    RefSeqiNP_000865.2. NM_000874.4. [P48551-2]
    NP_001276054.1. NM_001289125.1. [P48551-1]
    NP_001276055.1. NM_001289126.1. [P48551-3]
    NP_001276057.1. NM_001289128.1. [P48551-3]
    NP_997467.1. NM_207584.2. [P48551-2]
    NP_997468.1. NM_207585.2. [P48551-1]
    UniGeneiHs.708195.

    Genome annotation databases

    EnsembliENST00000342101; ENSP00000343289; ENSG00000159110. [P48551-3]
    ENST00000342136; ENSP00000343957; ENSG00000159110. [P48551-1]
    ENST00000382264; ENSP00000371699; ENSG00000159110. [P48551-2]
    ENST00000404220; ENSP00000384309; ENSG00000159110. [P48551-2]
    GeneIDi3455.
    KEGGihsa:3455.
    UCSCiuc002yrb.3. human. [P48551-2]
    uc002yrd.3. human. [P48551-1]
    uc002yrf.3. human. [P48551-3]

    Polymorphism databases

    DMDMi1352466.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13621.1. [P48551-1 ]
    CCDS13622.1. [P48551-2 ]
    PIRi I39073.
    S59501.
    RefSeqi NP_000865.2. NM_000874.4. [P48551-2 ]
    NP_001276054.1. NM_001289125.1. [P48551-1 ]
    NP_001276055.1. NM_001289126.1. [P48551-3 ]
    NP_001276057.1. NM_001289128.1. [P48551-3 ]
    NP_997467.1. NM_207584.2. [P48551-2 ]
    NP_997468.1. NM_207585.2. [P48551-1 ]
    UniGenei Hs.708195.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P48551.
    SMRi P48551. Positions 28-237.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109677. 10 interactions.
    DIPi DIP-945N.
    IntActi P48551. 13 interactions.
    MINTi MINT-196715.
    STRINGi 9606.ENSP00000343957.

    Chemistry

    ChEMBLi CHEMBL2364170.
    DrugBanki 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.

    PTM databases

    PhosphoSitei P48551.

    Polymorphism databases

    DMDMi 1352466.

    Proteomic databases

    MaxQBi P48551.
    PaxDbi P48551.
    PRIDEi P48551.

    Protocols and materials databases

    DNASUi 3455.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342101 ; ENSP00000343289 ; ENSG00000159110 . [P48551-3 ]
    ENST00000342136 ; ENSP00000343957 ; ENSG00000159110 . [P48551-1 ]
    ENST00000382264 ; ENSP00000371699 ; ENSG00000159110 . [P48551-2 ]
    ENST00000404220 ; ENSP00000384309 ; ENSG00000159110 . [P48551-2 ]
    GeneIDi 3455.
    KEGGi hsa:3455.
    UCSCi uc002yrb.3. human. [P48551-2 ]
    uc002yrd.3. human. [P48551-1 ]
    uc002yrf.3. human. [P48551-3 ]

    Organism-specific databases

    CTDi 3455.
    GeneCardsi GC21P034602.
    HGNCi HGNC:5433. IFNAR2.
    HPAi CAB025889.
    MIMi 602376. gene.
    610424. phenotype.
    neXtProti NX_P48551.
    PharmGKBi PA29671.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41946.
    HOGENOMi HOG000013219.
    HOVERGENi HBG053907.
    InParanoidi P48551.
    KOi K05131.
    OMAi IYIRLER.
    PhylomeDBi P48551.
    TreeFami TF335897.

    Enzyme and pathway databases

    Reactomei REACT_25162. Interferon alpha/beta signaling.
    REACT_25216. Regulation of IFNA signaling.
    SignaLinki P48551.

    Miscellaneous databases

    ChiTaRSi IFNAR2. human.
    EvolutionaryTracei P48551.
    GeneWikii IFNAR2.
    GenomeRNAii 3455.
    NextBioi 13610.
    PMAP-CutDB Q6FHD7.
    PROi P48551.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48551.
    Bgeei P48551.
    CleanExi HS_IFNAR2.
    Genevestigatori P48551.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR015373. Interferon_alpha/beta_rcpt_bsu.
    [Graphical view ]
    Pfami PF09294. Interfer-bind. 1 hit.
    PF01108. Tissue_fac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.

    Entry informationi

    Entry nameiINAR2_HUMAN
    AccessioniPrimary (citable) accession number: P48551
    Secondary accession number(s): A8KAJ4
    , D3DSE8, D3DSE9, Q15467, Q6FHD7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3